2c5l: Difference between revisions
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==Overview== | ==Overview== | ||
Ras proteins signal to a number of distinct pathways by interacting with, diverse effectors. Studies of ras/effector interactions have focused on, three classes, Raf kinases, ral guanylnucleotide-exchange factors, and, phosphatidylinositol-3-kinases. Here we describe ras interactions with, another effector, the recently identified phospholipase C epsilon, (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2), by NMR and the structure of the RA2/ras complex by X-ray crystallography., Although the similarity between ubiquitin-like folds of RA1 and RA2 proves, that they are homologs, only RA2 can bind ras. Some of the features of the, RA2/ras interface are unique to PLCepsilon, while the ability to make, contacts with both switch I and II regions of ras is shared only .. | Ras proteins signal to a number of distinct pathways by interacting with, diverse effectors. Studies of ras/effector interactions have focused on, three classes, Raf kinases, ral guanylnucleotide-exchange factors, and, phosphatidylinositol-3-kinases. Here we describe ras interactions with, another effector, the recently identified phospholipase C epsilon, (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2), by NMR and the structure of the RA2/ras complex by X-ray crystallography., Although the similarity between ubiquitin-like folds of RA1 and RA2 proves, that they are homologs, only RA2 can bind ras. Some of the features of the, RA2/ras interface are unique to PLCepsilon, while the ability to make, contacts with both switch I and II regions of ras is shared only with, phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest, that, in a cellular context, the RA2 domain, in a mode specific to, PLCepsilon, has a role in membrane targeting with further regulatory, impact on PLC activity. | ||
==About this Structure== | ==About this Structure== | ||
2C5L is a | 2C5L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, GTP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C5L OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ubiquitin superfold]] | [[Category: ubiquitin superfold]] | ||
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Revision as of 12:45, 5 November 2007
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STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS
Overview
Ras proteins signal to a number of distinct pathways by interacting with, diverse effectors. Studies of ras/effector interactions have focused on, three classes, Raf kinases, ral guanylnucleotide-exchange factors, and, phosphatidylinositol-3-kinases. Here we describe ras interactions with, another effector, the recently identified phospholipase C epsilon, (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2), by NMR and the structure of the RA2/ras complex by X-ray crystallography., Although the similarity between ubiquitin-like folds of RA1 and RA2 proves, that they are homologs, only RA2 can bind ras. Some of the features of the, RA2/ras interface are unique to PLCepsilon, while the ability to make, contacts with both switch I and II regions of ras is shared only with, phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest, that, in a cellular context, the RA2 domain, in a mode specific to, PLCepsilon, has a role in membrane targeting with further regulatory, impact on PLC activity.
About this Structure
2C5L is a Protein complex structure of sequences from Homo sapiens with MG, GTP and GOL as ligands. Active as Small monomeric GTPase, with EC number 3.6.5.2 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structural and mechanistic insights into ras association domains of phospholipase C epsilon., Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M, Mol Cell. 2006 Feb 17;21(4):495-507. PMID:16483931
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