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1dsy

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Revision as of 11:26, 20 November 2007 by OCA (Talk | contribs)
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1dsy, resolution 2.6Å

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C2 DOMAIN FROM PROTEIN KINASE C (ALPHA) COMPLEXED WITH CA2+ AND PHOSPHATIDYLSERINE

Overview

The C2 domain acts as a membrane-targeting module in a diverse group of, proteins including classical protein kinase Cs (PKCs), where it plays an, essential role in activation via calcium-dependent interactions with, phosphatidylserine. The three-dimensional structures of the Ca(2+)-bound, forms of the PKCalpha-C2 domain both in the absence and presence of 1, 2-dicaproyl-sn-phosphatidyl-L-serine have now been determined by X-ray, crystallography at 2.4 and 2.6 A resolution, respectively. In the, structure of the C2 ternary complex, the glycerophosphoserine moiety of, the phospholipid adopts a quasi-cyclic conformation, with the phosphoryl, group directly coordinated to one of the Ca(2+) ions. Specific recognition, of the phosphatidylserine is reinforced by additional hydrogen bonds and, hydrophobic interactions with protein residues in the vicinity of the, Ca(2+) binding region. The central feature of the PKCalpha-C2 domain, structure is an eight-stranded, anti-parallel beta-barrel with a molecular, topology and organization of the Ca(2+) binding region closely related to, that found in PKCbeta-C2, although only two Ca(2+) ions have been located, bound to the PKCalpha-C2 domain. The structural information provided by, these results suggests a membrane binding mechanism of the PKCalpha-C2, domain in which calcium ions directly mediate the phosphatidylserine, recognition while the calcium binding region 3 might penetrate into the, phospholipid bilayer.

About this Structure

1DSY is a Single protein structure of sequence from Rattus norvegicus with CA, PO4 and PSF as ligands. Full crystallographic information is available from OCA.

Reference

Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine., Verdaguer N, Corbalan-Garcia S, Ochoa WF, Fita I, Gomez-Fernandez JC, EMBO J. 1999 Nov 15;18(22):6329-38. PMID:10562545

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