1dsy
From Proteopedia
(New page: 200px<br /><applet load="1dsy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dsy, resolution 2.6Å" /> '''C2 DOMAIN FROM PROTEI...) |
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| - | [[Image:1dsy.jpg|left|200px]]<br /><applet load="1dsy" size=" | + | [[Image:1dsy.jpg|left|200px]]<br /><applet load="1dsy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dsy, resolution 2.6Å" /> | caption="1dsy, resolution 2.6Å" /> | ||
'''C2 DOMAIN FROM PROTEIN KINASE C (ALPHA) COMPLEXED WITH CA2+ AND PHOSPHATIDYLSERINE'''<br /> | '''C2 DOMAIN FROM PROTEIN KINASE C (ALPHA) COMPLEXED WITH CA2+ AND PHOSPHATIDYLSERINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The C2 domain acts as a membrane-targeting module in a diverse group of | + | 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== | ==About this Structure== | ||
| - | 1DSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA, PO4 and PSF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=PSF:'>PSF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Corbalan-Garcia, S.]] | [[Category: Corbalan-Garcia, S.]] | ||
[[Category: Fita, I.]] | [[Category: Fita, I.]] | ||
| - | [[Category: Gomez-Fernandez, J | + | [[Category: Gomez-Fernandez, J C.]] |
| - | [[Category: Ochoa, W | + | [[Category: Ochoa, W F.]] |
[[Category: Verdaguer, N.]] | [[Category: Verdaguer, N.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: protein kinase c]] | [[Category: protein kinase c]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:14 2008'' |
Revision as of 10:20, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 12:20:14 2008
