2ct9
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(New page: 200px<br /><applet load="2ct9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ct9, resolution 2.20Å" /> '''The crystal structur...)
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Revision as of 07:07, 21 November 2007
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The crystal structure of calcineurin B homologous proein 1 (CHP1)
Overview
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a, calcium-binding EF-hand protein that plays a role in membrane trafficking., It binds to multiple effector proteins, including Na(+)/H(+) exchangers, a, serine/threonine kinase, and calcineurin, potentially modulating their, function. The crystal structure of calcium-bound CHP1 from rat has been, determined at 2.2 Angstroms of resolution. The molecule has a compact, alpha-helical structure containing four EF-hands. The overall folding, topology of the protein is similar to that of the regulatory B subunit of, calcineurin and to that of calcium- and integrin-binding protein. The, calcium ion is coordinated in typical fashion in the third and fourth, EF-hands, but the first and second EF-hands contain no calcium ion. The, first EF-hand is maintained by internal interactions, and the second, EF-hand is stabilized by hydrophobic interactions. CHP1 contains a, hydrophobic pocket on the opposite side of the protein to the EF-hands, that has been implicated in ligand binding.
About this Structure
2CT9 is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural characterization of calcineurin B homologous protein 1., Naoe Y, Arita K, Hashimoto H, Kanazawa H, Sato M, Shimizu T, J Biol Chem. 2005 Sep 16;280(37):32372-8. Epub 2005 Jun 29. PMID:15987692
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