1a25
From Proteopedia
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:43:57 2007'' |
Revision as of 12:39, 30 October 2007
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C2 DOMAIN FROM PROTEIN KINASE C (BETA)
Overview
BACKGROUND: Conventional isoforms (alpha, beta and gamma) of protein, kinase C (PKC) are synergistically activated by phosphatidylserine and, Ca2+; both bind to C2 domains located within the PKC amino-terminal, regulatory regions. C2 domains contain a bipartite or tripartite, Ca2+-binding site formed by opposing loops at one end of the protein., Neither the structural basis for cooperativity between phosphatidylserine, and Ca2+, nor the binding site for phosphatidylserine are known. RESULTS:, The structure of the C2 domain from PKCbeta complexed with Ca2+ and, o-phospho-L-serine has been determined to 2.7 A resolution using X-ray, crystallography. The eight-stranded, Greek key beta-sandwich fold of, PKCbeta-C2 is similar to that of the synaptotagmin I type I C2 domain., Three Ca2+ ions, ... [(full description)]
About this Structure
1A25 is a [Single protein] structure of sequence from [Rattus norvegicus] with CA and PSE as [ligands]. Structure known Active Site: CLB. Full crystallographic information is available from [OCA].
Reference
Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+., Sutton RB, Sprang SR, Structure. 1998 Nov 15;6(11):1395-405. PMID:9817842
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