1a25: Difference between revisions
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[[Image:1a25.gif|left|200px]] | [[Image:1a25.gif|left|200px]] | ||
'''C2 DOMAIN FROM PROTEIN KINASE C (BETA)''' | {{Structure | ||
|PDB= 1a25 |SIZE=350|CAPTION= <scene name='initialview01'>1a25</scene>, resolution 2.70Å | |||
|SITE= <scene name='pdbsite=CLB:Ca+Binding+Site'>CLB</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''C2 DOMAIN FROM PROTEIN KINASE C (BETA)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A25 is a [ | 1A25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A25 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9817842 9817842] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:48 2008'' | ||
Revision as of 10:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
C2 DOMAIN FROM PROTEIN KINASE C (BETA)
OverviewOverview
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, one at a novel site, were located, each sharing common aspartate ligands. One of these ligands is donated by a dyad-related C2 molecule. A phosphoserine molecule binds to a lysine-rich cluster in C2. CONCLUSIONS: Shared ligation among the three Ca2+ ions suggests that they bind cooperatively to PKCbeta-C2. Cooperativity may be compromised by the accumulation of positive charge in the binding site as successive ions are bound. Model building shows that the C1 domain could provide carboxylate and carbonyl ligands for two of the three Ca2+ sites. Ca2+-mediated interactions between the two domains could contribute to enzyme activation as well as to the creation of a positively charged phosphatidylserine-binding site.
About this StructureAbout this Structure
1A25 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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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