Definition
A family of intracellular calcium-binding proteins, spread over all forms of life, from bacteria to vertebrate neuronal tissues, have a very similar three-dimensional structure, characteristic, and unique for this family, and involved in a variety of functions including intracellular calcium buffering, bioluminescence, enzymatic activity and associative learning.
Introduction
Calcium ions (Ca2+) are essential for the normal function of the cell. A transient rise of the intracellular Ca2+ concentration is achieved by its entering the cell through various plasma membrane Ca2+ channels and/or by being liberated from various internal stores after an appropriate stimulus. The rise and fall of intracellular Ca2+ is very versatile and different in different cell types, with very local ion gradients, hot spots, waves, and oscillations. Calcium-binding proteins(CaBP) have been...
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Collins JH, Johnson DJ, Szent-Gyorgyi AG (1983) Purification and characterization of a scallop sarcoplasmic calcium-binding protein. Biochemistry 22:341–345
Cook WJ, Jeffrey LC, Cox JA, Vijay-Kumar S (1993) Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J Mol Biol 229:461–471
Cox JA, Bairoch A (1988) Sequence similarities in calcium-binding proteins. Nature 331:491
Cox JA, Stein EA (1981) Characterisation of a new sarcoplasmic calcium-binding protein with magnesium-induced cooperativity in the binding of calcium. Biochemistry 20:5430–5436
Cox JA, Wnuk W, Stein EA (1976) Isolation and properties of a sarcoplasmic calcium-binding protein from crayfish. Biochemistry 15:2613–2618
Erskine PT, Beaven GDE, Hagan R, Findlow IS, Wermer JM, Wood SP, Vernon J, Giese KP, Fox G, Cooper JB (2006) Structure of the neuronal protein calexcitin suggests a mode of interaction in signalling pathways of learning and memory. J Mol Biol 357:1536–1547
Gombos Z, Durussel I, Ikura M, Rose DR, Cox JA, Chakrabartty A (2003) Conformational coupling of Mg2+ and Ca2+ on the three-state folding of calexcitin B. Biochemistry 42:5531–5539
Head JF, Inouye S, Teranishi K, Shimomura O (2000) The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature 405:372–376
Hermann A, Cox JA (1995) Sarcoplasmic calcium-binding proteins. Comp Biochem Physiol 111B:337–345
Nelson TJ, Zhao WQ, Yuan S, Favi A, Pozzo-Miller L, Alkon DL (1999) Calexcitin interacts with neuronal ryanodine receptors. Biochem J 341:423–433
Tossavainen H, Permi P, Annila I, Kilpelainen I, Drakenberg T (2003) NMR solution structure of calerythrin, an EF-hand calcium-binding protein of Saccharopolyspora erythraea. Eur J Biochem 270:2505–2512
Vijay-Kumar S, Cook WJ (1992) Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution. J Mol Biol 224:413–426
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media New York
About this entry
Cite this entry
Cox, J.A. (2013). Sarcoplasmic Calcium-Binding Protein Family: SCP, Calerythrin, Aequorin, and Calexcitin. In: Kretsinger, R.H., Uversky, V.N., Permyakov, E.A. (eds) Encyclopedia of Metalloproteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1533-6_68
Download citation
DOI: https://doi.org/10.1007/978-1-4614-1533-6_68
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-1532-9
Online ISBN: 978-1-4614-1533-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences