Chaperonins

Title: Chaperonins
Additional Names: Cpns
Literature References: Subset of molecular chaperone proteins, including the nucleoplasmins and heat shock proteins, that guide the in-vivo transport, folding and assembly of other protein structures but are not themselves components of these structures as part of their biological function. The term "chaperonin" was coined by S. M. Hemmingsen et al., Nature 333, 330 (1988) to describe the function of these proteins. Characterized by large oligomeric cage-like structures with multiple rings of subunits possessing 7,8 or 9-fold symmetry. Ubiquitous conserved proteins which have been identified in most microorganisms and cellular compartments, requires the interaction of two chaperonins to ensure correct folding: J. Martin et al., Nature 366, 228, 279 (1993). Molecular study of mechanism: S. G. Burston et al., J. Mol. Biol. 249, 138 (1995). Review: R. J. Ellis, S. M. van der Vies, Annu. Rev. Biochem. 60, 321-347 (1991). Review of structures and conformations: H. Saibil, S. Wood, Curr. Opin. Struct. Biol. 3, 207-213 (1993). Review of E. coli chaperonins, cpn60-cpn10: F. Baneyx, Ann. N.Y. Acad. Sci. 745, 383-394 (1994).
Chartreusin Charybdotoxin Chaulmoogra Oil Chaulmoogric Acid Chavicine

Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional form. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones.[1] The energy to fold proteins is supplied by adenosine triphosphate (ATP).