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2c5l
From Proteopedia
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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 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. | 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. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Bladder cancer, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190020 190020]], Costello syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190020 190020]], Thyroid carcinoma, follicular, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190020 190020]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: ubiquitin superfold]] | [[Category: ubiquitin superfold]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:10:49 2007'' |
Revision as of 19:04, 12 November 2007
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STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS
Contents |
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.
Disease
Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]
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
Page seeded by OCA on Mon Nov 12 21:10:49 2007
Categories: Homo sapiens | Protein complex | Small monomeric GTPase | Bunney, T.D. | Katan, M. | Pearl, L.H. | Roe, S.M. | GOL | GTP | MG | Disease mutation | Gtp-binding | Lipoprotein | Nucleotide-binding | Oncogene | Palmitate | Prenylation | Proto-oncogene | Ras | Signaling protein | Ubiquitin superfold
