2c5l

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{{STRUCTURE_2c5l| PDB=2c5l | SCENE= }}
{{STRUCTURE_2c5l| PDB=2c5l | SCENE= }}
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'''STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS'''
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===STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 16483931 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16483931}}
==About this Structure==
==About this Structure==
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[[Category: Signaling protein]]
[[Category: Signaling protein]]
[[Category: Ubiquitin superfold]]
[[Category: Ubiquitin superfold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:17:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:33:50 2008''

Revision as of 13:33, 28 July 2008

Image:2c5l.png

Template:STRUCTURE 2c5l

STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS

Template:ABSTRACT PUBMED 16483931

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

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