Review Articles and Other Starting Points for Information About Calcium-Binding Proteins

Broad Surveys and Comparative Studies

The EF-Hand Motif

• Kretsinger, R.H., D. Tolbert, S. Nakayama, W. Pearson. The EF-hand, homologs and analogs, in Novel Calcium-Binding Proteins: Fundamentals and Clinical Implications, C.W. Heizmann, ed. (1991) Springer-Verlag, New York, 17-37.
  Covers the canonical EF-hand motif, as well as the more common variants, including the pseudo-EF-hand.

Survey of Various Proteins

• Celio, M.R., T. Pauls, B. Schwaller, eds. Guidebook to the Calcium-Binding Proteins (1996) Oxford University Press, Oxford.
  Contains short reviews on many calcium-binding proteins. An excellent starting place in a search for information about a particular protein.

Structural Aspects of Calcium-Binding Proteins

• Nelson, M.R., W.J. Chazin. Structures of EF-Hand Ca2+-binding proteins: Diversity in the organization, packing, and response to Ca2+ binding (1998) BioMetals 11, 297-318.
  This review covers the structures of classical calcium sensors (calmodulin and troponin C) and buffers (calbindin D9k and parvalbumin), as well as the myosin light chains, S100 proteins, recoverin, calpain domain VI, sarcoplasmic calcium-binding proteins, and SPARC.
• Ikura, M. Calcium binding and conformational response in EF-hand Proteins (1996) Trends Biochem. Sci. 21, 14-17.
  A short review about the relationships between calcium-binding, structure, and function in EF-hand calcium-binding proteins.
• McPhalen, C.A., N.C.J. Strynadka, M.N.G. James. Calcium-binding sites in proteins: A structural perspective (1991) Adv. Prot. Chem. 42, 77-144.
  A thorough, although slightly out of date, review of the structural details of calcium-binding sites in both EF-hand calcium-binding proteins and other types of calcium-binding proteins.
• Nelson, M.R., W.J. Chazin. An interaction-based analysis of calcium-induced conformational changes in Ca²⁺ sensor proteins (1998) Protein Sci. 7, 270-282.
  This research article gives detailed descriptions of the calcium-induced conformational changes in the classical calcium sensors calmodulin and troponin C, and discusses the implications of these changes for the understanding of the relationship between structure and function in EF-hand calcium-binding proteins.
• Chazin, W.J. Releasing the calcium trigger (1995) Nature Struct. Biol. 2, 707-710.
  A news and views article assessing the impact of the NMR structures of apo calmodulin and troponin C, and discussing the insight these structures provide into the biological functions of these proteins.

Evolutionary Relationships of Calcium-Binding Proteins

• Nakayama, S., Kretsinger, R.H. Evolution of the EF-hand family of proteins (1994) Annu. Rev. Biophys. Biomol. Struct. 23, 473-507.
  Review of the evolutionary relationships of EF-hand calcium-binding proteins and their chromosomal locations.

Specific Proteins and Subfamilies

C2 Domains

• Nalfeski, E.A., J.J. Falke. The C2 domain calcium-binding motif: Structural and functional diversity (1996) Protein Sci. 5, 2375-2390.
  

Calcineurin

• Guerini, D. Calcineurin: not just a simple protein phosphatase (1997) Biochem. Biophys. Res. Comm. 235, 271-275.
  A short, but very useful, review

Calcium-Dependepnt Protein Kinase

• Roberts, D.M. Protein kinases with calmodulin-like domains: novel targets of calcium signals in plants (1993) Curr. Opin. Cell Biol. 5, 242-246
  A concise introduction to calcium-dependent protein kinase in plants
• Roberts, D.M., A.C. Harmon. Calcium-modulated proteins: targets of intracellular calcium signals in higer plants (1992) Annu. Rev. Plant Physiol Plant Mol Biol. 43, 375-414.
  A more thorough discussion of calcium-dependent protein kianses. This review also discusses calmodulin in plants.

Calmodulin

• O'Neill, K.T., W.F. DeGrado. How calmodulin binds it targets: sequence independent recognition of amphiphilic alpha-helices (1990) Trends Biochem. Sci. 15, 59-64.
  An excellent review of the theory explaining the ability of calmodulin to interact strongly with a wide-range of targets.
• Crivici, A., M. Ikura. Molecular and structural basis of target recognition by calmodulin (1995) Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
  A more thorough review of the interaction of calmodulin with targets.
• Nelson, M.R., W.J. Chazin. Calmodulin as a calcium sensor, in Calmodulin and Signal Transduction, L.J. Van Eldik and D.M. Watterson, eds. (1998) Academic Press, San Diego, 17-64.
  An introduction to the structural aspects of calmodulin and its function as a calcium sensor.
• Roberts, D.M., A.C. Harmon. Calcium-modulated proteins: targets of intracellular calcium signals in higer plants (1992) Annu. Rev. Plant Physiol Plant Mol Biol. 43, 375-414.
  A good introduction to calmodulin in higher plants. The review also discusses calcium-dependent protein kinases.

Calpain

• Croall, D.E., G.N. Demartino. Calcium-activated neutral protease (calpain) system: structure, function, and regulation (1991) Physiol. Rev. 71, 813-847.
  A very thorough and careful review.
• Wang, K.K.W., P.-W. Yuan. Calpain inhibition: an overview of its therapeutic potential (1994) Trends Pharm. Sci. 15, 412-419.
  This review is good for information about possible biological roles of calpain
• Goll, D.E., V.F. Thompson, R.G. Taylor, T. Zalewska (1992) BioEssays 14, 549-556.
  Reviews the controversy about how calpain activity is regulated, and argues that the hypothesis that calpain is regulated by membranes and autolysis is unable to explain all of the experimental data.

Caltractin/Centrin

• Schiebel, E., M. Bornens. In search of a function for centrins (1995) Trends Cell Biol. 5, 197-201.
  

MRP-8 and MRP-14 (S100A8 and S100A9)

• Hessian, P.A, J. Edgeworth, N. Hogg. MRP-8 and MRP-14, two abundant Ca²⁺-binding proteins of neutrophils and monocytes (1993) J. Leuk. Biol. 53, 197-204.

Parvalbumin

• Pauls, T.L., J.A. Cox, M.W. Brechtold. The Ca²⁺-binding proteins parvalbumin and oncomodulin and their genes: new structural and functional findings (1996) Biochim. Biophys. Acta 1306, 39-54.
  An excellent review of the function, genetics, and structures of parvalbumins.

Recoverin

• Ames, J.B., T. tanaka, L. Stryer, M. Ikura. Portrait of a myristoyl switch protein (1996) Curr. Opin. Struct. Biol. 6, 432-438.
  This review predates the structure of calcium-loaded, myristoylated recoverin, but many of the hypotheses put forward were supported by this structure when it became available.

S100 Proteins

• Schafer, B.W., C.W. Heizmann. The S100 family of EF-hand calcium-binding proteins: functions and pathology (1996) Trends Biochem. Sci. 21, 134-140.
  A useful review about the roles of S100 proteins in both normal cell function and disease states.

SPARC/BM-40/Osteonectin

• Lane, T.F., E.H. Sage. The biology of SPARC, a protein that modulates cell-matrix interactions (1994) FASEB J. 6, 163-173.
  

Troponin C

• Farah, C.S., F.C. Reinach. The troponin complex and regulation of muscle contraction (1995) FASEB J. 9, 755-767.
  

Biological Function

Calcium-Binding Proteins and Disease

• Heizmann, C.W., K. Braun. Changes in Ca²⁺-binding proteins in human neurodegenerative disorders (1992) Trends Neuro. Sci. 15, 259-264.
  A review summarizing knowledge about the role of parvalbumin and calbindin D_28K in protecting the brain from damage.

Intracellular Calcium Signalling

• Bootman, M.D., M.J. Berridge. The elemental principles of calcium signaling (1995) Cell, 83, 675-678.
  A minireview describing fundamental units of the calcium signal in various systems and postualting on the roles of the many complex types of calcium signal in biology.

Biophysical Aspects

Affinity and Cooperativity of Calcium Binding

• Linse, S., S. Forsen. Determinants that govern high-affinity calcium binding (1995) Adv. Sec. Mess. Phos. Res. 30, 89-150.
  Excellent and detailed discussion of calcium affinity and cooperativity, particularly in EF-hand calcium-binding proteins.
• Forsen, S., S. Linse. Cooperativity: over the Hill (1995) Trends Biochem. Sci. 20, 495-497.
  Short paper presenting the rigorous definition of cooperativity of binding events, and arguing against the use of the Hill coefficient. An outstanding introduction to cooperativity.

The references on this page are intended to provide a starting point for the study of calcium-binding proteins. This list is in no way intended to be comprehensive, and certainly reflects the bias of the data library administrator. See the index of the references subsection for more complete reference lists. Submissions of additional references are welcome. Please e-mail the complete reference, and a short description of the reference to the library administrator.

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