2c5l | pdb_00002c5l

Structure of PLC epsilon Ras association domain with hRas

spinqualitylabelsall models 2c5l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: GOL, GTP, MG 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GTPase Hras 3D structures

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