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2chd
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(New page: 200px<br /> <applet load="2chd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2chd, resolution 1.92Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 18:30, 29 October 2007
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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 ... [(full description)]
About this Structure
2CHD is a [Single protein] structure of sequence from [Rattus norvegicus] with GOL as [ligand]. 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
Page seeded by OCA on Mon Oct 29 20:35:20 2007
