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2c5l
From Proteopedia
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[[Image:2c5l.gif|left|200px]] | [[Image:2c5l.gif|left|200px]] | ||
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'''STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS''' | '''STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS''' | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Roe, S M.]] | [[Category: Roe, S M.]] | ||
| - | [[Category: | + | [[Category: Disease mutation]] |
| - | [[Category: | + | [[Category: Gtp-binding]] |
| - | [[Category: | + | [[Category: Lipoprotein]] |
| - | [[Category: | + | [[Category: Nucleotide-binding]] |
| - | [[Category: | + | [[Category: Oncogene]] |
| - | [[Category: | + | [[Category: Palmitate]] |
| - | [[Category: | + | [[Category: Prenylation]] |
| - | [[Category: | + | [[Category: Proto-oncogene]] |
| - | [[Category: | + | [[Category: Ra]] |
| - | [[Category: | + | [[Category: Signaling protein]] |
| - | [[Category: | + | [[Category: Ubiquitin superfold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:17:17 2008'' | |
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Revision as of 18:17, 3 May 2008
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. 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 Sat May 3 21:17:17 2008
