| Structural highlights
2c5l is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Ligands: | , , |
Related: | 121p, 1aa9, 1agp, 1bkd, 1clu, 1crp, 1crq, 1crr, 1ctq, 1gnp, 1gnq, 1gnr, 1he8, 1iaq, 1ioz, 1jah, 1jai, 1k8r, 1lf0, 1lf5, 1lfd, 1nvu, 1nvv, 1nvw, 1nvx, 1p2s, 1p2t, 1p2u, 1p2v, 1plj, 1plk, 1pll, 1q21, 1qra, 1rvd, 1wq1, 1xcm, 1xd2, 1xj0, 221p, 2gdp, 2q21, 421p, 4q21, 521p, 5p21, 621p, 6q21, 721p, 821p |
Activity: | Small monomeric GTPase, with EC number 3.6.5.2 |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Structural and mechanistic insights into ras association domains of phospholipase C epsilon. Mol Cell. 2006 Feb 17;21(4):495-507. PMID:16483931 doi:http://dx.doi.org/10.1016/j.molcel.2006.01.008
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