2BYF
NMR solution structure of phospholipase c epsilon RA 2 domain
Summary for 2BYF
Entry DOI | 10.2210/pdb2byf/pdb |
Related | 2BYE |
NMR Information | BMRB: 6635 |
Descriptor | PHOSPHOLIPASE C, EPSILON 1 (1 entity in total) |
Functional Keywords | phospholipase c epsilon, ras binding domain, ubiquitin superfold, lipase |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 1 |
Total formula weight | 13106.79 |
Authors | Bunney, T.D.,Harris, R.,Gandarillas, N.L.,Josephs, M.B.,Roe, S.M.,Paterson, H.F.,Rodrigues-Lima, F.,Esposito, D.,Gieschik, P.,Pearl, L.H.,Driscoll, P.C.,Katan, M. (deposition date: 2005-08-01, release date: 2006-02-22, Last modification date: 2024-06-19) |
Primary citation | Bunney, T.D.,Harris, R.,Gandarillas, N.L.,Josephs, M.B.,Roe, S.M.,Sorli, S.C.,Paterson, H.F.,Rodrigues-Lima, F.,Esposito, D.,Ponting, C.P.,Gierschik, P.,Pearl, L.H.,Driscoll, P.C.,Katan, M. Structural and Mechanistic Insights Into Ras Association Domains of Phospholipase C Epsilon. Mol.Cell, 21:495-, 2006 Cited by PubMed Abstract: 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. PubMed: 16483931DOI: 10.1016/J.MOLCEL.2006.01.008 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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