2chd
From Proteopedia
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CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A
Overview
Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal, structure of the Ca2+-free C2A domain has been solved by molecular, replacement and refined to 1.92 A resolution. It adopts the classical, C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich, with type I topology. In agreement with its Ca2+-dependent negatively, charged membrane-binding properties, this C2 domain contains all the, conserved acidic residues responsible for calcium binding. However, the, replacement of a conserved aspartic acid residue by glutamic acid allows, formation of an additional strong hydrogen bond, resulting in increased, rigidity of calcium-binding loop 1. The electrostatic surface of the C2A, domain consists of a large positively charged belt surrounded by two, negatively charged patches located at both tips of the domain. In, comparison, the structurally very similar C2A domain of synaptotagmin I, has a highly acidic electrostatic surface, suggesting completely unrelated, functions for these two C2A domains.
About this Structure
2CHD is a Single protein structure of sequence from Rattus norvegicus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:16790935
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