1dsy
From Proteopedia
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|PDB= 1dsy |SIZE=350|CAPTION= <scene name='initialview01'>1dsy</scene>, resolution 2.6Å | |PDB= 1dsy |SIZE=350|CAPTION= <scene name='initialview01'>1dsy</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PSF:1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE'>PSF</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsy OCA], [http://www.ebi.ac.uk/pdbsum/1dsy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dsy RCSB]</span> | ||
}} | }} | ||
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[[Category: Ochoa, W F.]] | [[Category: Ochoa, W F.]] | ||
[[Category: Verdaguer, N.]] | [[Category: Verdaguer, N.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: PSF]] | ||
[[Category: calcium++]] | [[Category: calcium++]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
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[[Category: protein kinase c]] | [[Category: protein kinase c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:06 2008'' |
Revision as of 16:48, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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