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http://purl.uniprot.org/citations/9817842http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9817842http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9817842http://www.w3.org/2000/01/rdf-schema#comment"

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."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(98)00139-7"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(98)00139-7"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/author"Sutton R.B."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/author"Sutton R.B."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/author"Sprang S.R."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/author"Sprang S.R."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/pages"1395-1405"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/pages"1395-1405"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/title"Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/title"Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+."xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/9817842http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/9817842http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9817842
http://purl.uniprot.org/citations/9817842http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9817842
http://purl.uniprot.org/citations/9817842http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9817842
http://purl.uniprot.org/citations/9817842http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9817842
http://purl.uniprot.org/uniprot/P68403http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9817842
http://purl.uniprot.org/uniprot/P68403#attribution-E618C29D0FAD4510FD5D3597117C5904http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9817842
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