References about Calbindin D9k

References about Calbindin D9k

Please note: this is not intended to be a complete listing of references.

See the home page for Calbindin D9k for more information.

Akke, M., Bruschweiler, R., Palmer, A.GN., III. NMR order parameters and free energy: An analytical approach and its application to cooperative Ca2+ binding by calbindin D9k (1993) J Am Chem Soc 115, 9832-9833.
No information from this reference is currently stored in the database

Akke, M., Drakenberg, T., Chazin, W.J Three-dimensional solution structure of Ca2+-loaded porcine calbindin D9k determined by nuclear magnetic resonance spectroscopy (1992) Biochemistry 31, 1011-1020.
Summary: The reference for pdb entry 1CB1.
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Akke, M., Forsen, S., Chazin, W. Solution structure of (Cd(2+)1-calbindin D9k reveals details of the stepwise structural changes along the apo -> (Ca(2+))II,1 -> (Ca(2+))I,II,2 binding pathway (1995) J Mol Biol 252, 102-121.
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Akke, M., Forsen, S., Chazin, W.J Molecular basis for cooperativity in Ca2+ binding in calbindin D9k (1991) J Mol Biol 220, 173-189.
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Akke, M., Skelton, N.J, Kordel, J., Palmer, A.GN., III., Chazin, W.J Effects of ion binding on the backbone dynamics of calbindin D9k determined by 15N NMR relaxation (1993) Biochemistry 32, 9832-9844.
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Andersson, M., Malmendal, A., Linse, S., Ivarsson, I., Forsen, S., Svensson, L.A Structural basis for the negative allostery between Ca2+- and Mg2+-binding to the intacellular Ca2_-receptor calbindin D9k (1997) Protein Sci 6, 1139-1147.
Summary: Presents the crystal structures of calbindin D9k with either one magneisum or one manganese ion bound to site II. These two structures adopt similar conformations, unique from the apo or Ca2+-loaded conformations of calbindin. The paper also presents Mg2+-binding constants and Ca2+ constants measured in the presence of Mg2+..
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Balmain, N. Calbindin D(9k): A vitamin D dependent, calcium-binding protein in mineralized tissues (1991) Clin Orthop 265, 265-276.
Summary: A summary of what is known about the role of calbindin in bones and teeth..
No information from this reference is currently stored in the database

Brodin, P., Drakenberg, T., Thulin, E., Forsen, S., Grundstrom, T. Selective proton labelling of amino acids in deuterated bovine calbindin D9k. A way to simplify (1)H-NMR spectra (1989) Protein Eng 2, 353-358.
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Brodin, P., Grundstrom, T., Hofmann, T., Drakenberg, T., Thulin, E., Forsen, S. Expression of bovine intenstinal calcium binding protein from a synthetic gene in Escherichia coli and characterization of the product (1986) Biochemistry 25, 5371-5377.
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Brodin, P., Johansson, C., Forsen, S., Drakenberg, T., Grundstrom, T. Functional properties of calbindin D9k mutants with exchanged Ca(2+) binding sites (1990) J Biol Chem 265, 11125-11130.
Summary: Three mutants were made: one with two site I binding loops (mutant A), one with two site II binding loops (mutant B), and one with the site I and site II loops exchanged (mutant C). All three mutants bind calcium-- mutant B has a decrease in affinity (with respect to wildtype) of about one order of magnitude, while mutants A and C have a decrease in affinity of about two orders of magnitude. Cooperativity of binding is lost in all three mutants..
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Bronner, F., Pansu, D., Stein, W.F An analysis of intestinal calcium transport across the rat intestine (1986) Am J Physiol 150G, 561-569.
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Bruns, M.E, Kleeman, E., Bruns, D.E Vitamin D-dependent calcium-binding protein of mouse yolk sac (1986) J Biol Chem 261, 7485-7490.
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Bruns, M.E, Overpeck, J.G, Smith, G.C, Hirsch, G.N, Mills, S.E Vitamin D-dependent calcium binding protein in rat uterus: differential effects of estrogen, tamoxifen, progesterone and pregnancy on accumulation and cellular localization (1988) Endocrinology 122, 2371-2378.
Summary: A study of the localization of calbindin D9k in uterine tissues of pregnant rats and hormone-treated non-pregnant rats. Estrogen only partially mimcs the effects of pregnancy on calbindin distribution.
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Carlstrom, G., Chazin, W.J Two-dimensional (1)H nuclear magnetic resonance studies of the half-saturated (Ca(2+))1 state of calbindin D9k: further implications for the molecular basis of cooperative Ca(2+) binding (1993) J Mol Biol 231, 415-430.
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Chazin, W.J, Kordel, J., Thulin, E., Hoffmann, T., Drakenberg, T., Forsen, S. Identification of an isoaspartyl linkage formed upon deamidation of bovine calbindin D9k and structural characterization by 2D 1H NMR (1989) Biochemistry 28, 8646-8653.
No information from this reference is currently stored in the database

Christakos, S., Gabrielides, C., Rhoten, W.B Vitamin D-dependent calcium binding proteins: chemistry, distribution, functional considerations, and molecular biology (1989) Endoc Rev 10, 3-26.
Summary: A very useful summary of information about the biology and function of calbindin D28k and calbindin D9k..
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Delorme, A.C, Danan, J.L, Acker, M.G, Ripoche, M.A, Mathieu, H. In rat uterus 17 beta-estradiol stimulates a calcium-binding protein similar to the duodenal vitamin D-dependent calcium-binding protein (1983) Endocrinology 113, 1340-1347.
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Denisov, V.P, Halle, B. Direct observation of calcium-coordinated water in calbindin D9k by nuclear magnetic relaxation dispersion (1995) J Am Chem Soc 117, 8456-8465.
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Feher, J.J Facilitated calcium diffusion by intestinal calcium-binding protein (1983) Am J Physiol 244C, 303-307.
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Finn, B.E, Kordel, J., Thulin, E., Sellers, P., Forsen, S. Dissection of calbindin D9k into two Ca2+-binding subdomains by a combination of mutagenesis and chemical cleavage (1992) FEBS Lett 298, 211-214.
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Forsen, S., Kordel, J., Grundstrom, T., Chazin, W.J The molecular anatomy of a calcium-binding protein (1993) Acc Chem Res 26, 7-14.
No information from this reference is currently stored in the database

Fullmer, C.S, Wasserman, R.H The amino acid sequence of bovine intestinal calcium-binding protein (1981) J Biol Chem 256, 5669-5674.
Summary: The first report of the sequence of calbindin D9k, done at the amino acid level..
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Groves, P., Finn, B.E, Kuznicki, J., Forsen, S. A model for target proteins binding to calcium-activated S100 dimers1 (1998) FEBS Lett 421, 175-179.
Summary: Presents a hypothesis about the mode by which S100 proteins interact with targets based on a mutant of calbindin D9k with an insertion in the linker loop.
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Groves, P., Linse, S., Thulin, E., Forsen, S. A calbindin D9k mutant containing a novel structural extension: (1)H nuclear magentic resonance studies (1997) Protein Sci 6, 323-330.
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Hersmdorf, C.L, Bronner, F. Vitamin D-dependent calcium-binding protein from rat kidney (1985) Biochim Biophys Acta 379, 553-561.
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Howard, A., Legon, S., Spurr, N.K, Walters, J.RF. Molecular cloning and chromosomal assignment of human calbindin-D9k (1992) Biochem Biophys Res Comm 185, 663-669.
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Johansson, C., Brodin, P., Grundstrom, T., Forsen, S., Drakenberg, T. Mutation of the pseudo-EF hand of calbindin D9k into a normal EF hand: biophysical studies (1991) Eur J Biochem 202, 1283-1290.
Summary: A series of mutants were made in an attempt to turn the pseudo-EF hand loop into a canonical one. One mutant (A14 removed+A15D+P20G+N21 removed) seems to do this, but cooperativity is lost..
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Johansson, C., Brodin, P., Grundstrom, T., Thulin, E., Forsen, S., Drakenberg, T. Biophysical studies of engineered mutant proteins based on calbindin D9k modified in the pseudo EF-hand (1990) Eur J Biochem 187, 455-460.
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Johansson, C., Ullner, M., Drakenberg, T. The solution structures of mutant calbindin D9k¹s, as determined by NMR, show that the calcium-binding site can adopt different folds. (1993) Biochemistry 32, 8429-8438.
Summary: Report of the NMR structure of a mutant calbindin in which the N terminal binding loop is converted from a pseudo-EF hand to a canonical fold. The mutant is A14 removed+A15D+P20G+N21 removed+P43M. The calcium-loaded state of this mutant is found to have the same global fold (³closed²) as the wildtype protein. The proton assignments indicate that the mutant A14 removed+P20G+N21 removed also adopts the canonical fold..
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Julenius, K., Thulin, E., Linse, S., Finn, B.E Hydrophobic core substitutions in calbindin D9k: effects on stability and structure (1998) Biochemistry 37, 8915-8925.
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Kesvatera, T., Jonsson, B., Thulin, E., Linse, S. Binding of Ca(2+) to calbindin D9k: structural stability and function at high salt concentration (1994) Biochemistry 33, 14170-14176.
Summary: Calbindin retains its structure and ability to bind calcium in 1M KCl. Studies with high salt and charge-neutralizing mutations indicate that cooperativity of calcium binding is greatly influenced by electrostatics..
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Kordel, J., Forsen, S., Drakenberg, T., Chazin, W.J The rate and structural consequences of proline cis-trans isomerization in calbindin D9k: NMR studies of the minor (Cis-Pro43) isoform and the Pro43Gly mutant (1990) Biochemistry 29, 4000-4009.
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Kordel, J., Pearlman, D.A, Chazin, W.J Protein solution structure calculations in solution: Solvated molecular dynamics refinement of calbindin D9k (1997) J Biomol NMR 10, 231-243.
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Kordel, J., Skelton, N., Akke, M., Chazin, W.J High resolution solution structure of calcium-loaded calbindin D9k (1993) J Mol Biol 231, 711-734.
Summary: Presents the solution structure of calcium loaded calbindin and makes a useful comparison with the crystal structure.
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Kordel, J., Skelton, N.J, Akke, M., Palmer, A.G, Chazin, W.J Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy (1992) Biochemistry 31, 4856-4866.
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Kragelund, B.B, Jonsson, M., Bifulco, G., Chazin, W.J, Nilsson, H., Finn, B.E, Linse, S. Hydrophobic core substitution in calbindin D9k: Effects on Ca2+ binding and dissociation (1998) Biochemistry 37, 8926-8937.
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Linse, S., Brodin, P., Drakenberg, T., Thulin, E., Sellers, P., Elmden, K., Grundstrom, T., Forsen, S. Structure-function relationships in EF-Hand Ca(2+)-binding proteins. Protein engineering and biophysical studies of calbindin D9k (1987) Biochemistry 26, 6723-6735.
Summary: The mutation of Y13F has no effect on the cooperativity of calcium-binding, although it does affect the macroscopic binding constants..
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Linse, S., Bylsma, N.R, Drakenberg, T., Sellers, P., Forsen, S., Thulin, E. A calbindin D9k mutant with reduced calcium affinity and enhanced cooperativity. Metal ion binding, stability, and structural studies (1994) Biochemistry 33, 12478-12486.
Summary: Mutating glu 60 to asp decreases calcium affinity and increases cooperativity of binding. The decrease in affinity is thought to occur because the shorter asp side chain has a weaker hydrogen bond to the calcium-liganding water molecule thatn the glu side chain had. The reason for the increase in cooperativity is less apparent..
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Linse, S., Johansson, C., Brodin, P., Grundstrom, T., Drakenberg, T., Forsen, S. Electrostatic contributions to the binding of Ca(2+) in calbindin D9k (1991) Biochemistry 30, 154-183.
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Linse, S., Jonsson, B., Chazin, W.J The effect of protein concentration on ion binding (1995) Proc Natl Acad Sci USA 92, 4748-4752.
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Linse, S., Teleman, O., Torbjorn, D. Ca(2+) binding to calbindin D9k strongly affects backbone dynamics: measurements of exchange rates of individual amide protons using (1)H-NMR (1990) Biochemistry 29, 5925-5934.
Summary: Reports the measurement of exchange rates for all amide hydrogens in the calcium-loaded form of calbindin and about one-half pf the amide hydrogens in the apo form. In general, the calcium-loaded form has slower exchange..
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Linse, S., Thulin, E., Selllers, P. Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies (1993) Protein Sci 2, 985-1000.
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Malmendal, A., Carlstrom, G., Hambraeus, C., Drakenberg, T., Forsen, S., Akke, M. Sequence and context dependence of EF-hand loop dynamics. An (15)N relaxation study of a calcium-binding site mutant of calbindin D9k (1998) Biochemistry 37, 2586-2595.
No information from this reference is currently stored in the database

Marchand, S., Roux, B. Molecular dynamics study of calbindin D9k in the apo and singly and doubly calcium-loaded states (1998) Proteins 33, 265-284.
Summary: Describes molecular dynamics calculations on the apo, singly, and doubly calcium-laoded states of calbindin D9k, and relates the flucuations to experimental parameters of protein dynamics.
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Martin, S.R, Linse, S., Johansson, C., Bayley, P.M, Forsen, S. Protein surface charges and Ca(2+) binding to individual sites in calbindin D9k: stopped flow studies (1990) Biochemistry 29, 4188-4193.
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Nelson, M.R, Chazin, W.J An interaction-based analysis of calcium-induced conformational changes in Ca2+ sensor proteins (1998) Protein Sci 7, 270-282.
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Perret, C., Lomri, N., Gouhier, N., Auffray, C., Thomasset, M. The rat vitamin D-dependent calcium-binding protein (9-kDa CaBP) gene. Complete nucleotide sequence and structural organization (1988) Eur J Biochem 172, 43-51.
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Potts, B.CM., Carlstrom, G., Okazaki, K., Hidaka, H., Chazin, W.J (1)H NMR assignments of apo and comparative structural analysis with calbindin D9k and S100b (1996) Protein Sci 5, 2162-2174.
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Skelton, N.J, Akke, M., Kordel, J., Thulin, E., Forsen, S., Chazin, W.J 15N NMR assignment and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states. (1992) FEBS Lett 303, 136-140.
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Skelton, N.J, Forsen, S., Chazin, W.J (1)H NMR resonance assignments, secondary structure, and global fold of apo bovine calbindin (1990) Biochemistry 29, 5752-5761.
Summary: Sequence assignment and preliminary structural work on apo calbindin indicates that it has the same basic tertiary structure as the calcium-loaded state, but changed dynamics..
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Skelton, N.J, Kordel, J., Akke, M., Chazin, W.J Nuclear magnetic resonance studies of the internal dynamics in apo, (Cd(2+))1 and (Ca(2+))2 calbindin D9k (1992) J Mol Biol 227, 1100-1117.
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Skelton, N.J, Kordel, J., Chazin, W.J Determination of the solution structure of apo calbindin D9k by NMR spectroscopy (1995) J Mol Biol 249, 441-462.
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Svensson, B., Jonsson, B., Woodward, C. Electrostatic contributions to the binding of Ca(2+) in calbindin mutants: A Monte Carlo study (1990) Biophys J 38, 179-183.
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Svensson, B., Jonsson, B., Woodward, C.E, Linse, S. Ion-binding properties of calbindin D9k: a Monte Carlo simulation study (1991) Biochemistry 30, 5209-5217.
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Svensson, L.A, Thulin, E., Forsen, S. Proline cis-trans isomers in calbindin D9k observed by x-ray crystallography (1992) J Mol Biol 223, 601-606.
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Szebenyi, D.ME., Moffat, K. The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine (1986) J Biol Chem 261, 8761-8777.
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Szebenyi, D.ME., Obendorf, S.K, Moffat, K. Structure of vitamin D-dependent calcium-binding protein from bovine intestine (1981) Nature 294, 327-332.
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Thomasset, M., L'Horset, F., Blin, C., Lambert, M., Colnot, S., Perret, C. "Calbindin-D9k" in Guidebook to the Calcium-Binding Proteins, M.R.Celio, T.Pauls, B.Schwaller, eds. (1996) Oxford University Press, Oxford. 157-159.
Summary: A brief chapter summarizing the basic properties of calbindin D9k.
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Tsuji, T., Kaiser, E.T Design and synthesis of the pseudo-EF hand in calbindin D9k: effect of amino acid substitutions in the alpha-helical regions (1991) Proteins 9, 12-22.
Summary: Reports on a series of synthetic peptides of the pseudo EF-hand of calbindin D9k. The only modification found to increase Ca2+ affinity was the introduction of a disulfide bond.
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Wendt, B., Hofmann, T., Martin, S.R, Bayley, P., Brodin, P., Grundstrom, T., Thulin, E., Linse, S., Forsen, S. Effect of amino acid substitutions and deletions on the thermal stability and unfolding by urea of bovine calbindin D9k (1988) Eur J Biochem 175, 439-445.
Summary: A report of studies on the temperature and urea stability of the apo form of the following mutants: P20G, N21 removed, P20 removed, Y13F, E17Q, and on the the pH stability of the calcium-loaded states of the same mutants. Little or no change in the stabilities (with respect to wildtype) is found..
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Wimberly, B., Thulin, E., Chazin, W. Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant (1995) Protein Sci 4, 1045-1055.
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