2BYE

NMR solution structure of phospholipase c epsilon RA 1 domain

2BYE の概要

• エントリーDOI: 10.2210/pdb2bye/pdb
• 関連するPDBエントリー: 2BYF
• NMR情報: BMRB: 6624
• 分子名称: PHOSPHOLIPASE C, EPSILON 1 (1 entity in total)
• 機能のキーワード: phospholipase c epsilon, ras association domain, ubiquitin superfold, lipase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12804.60

構造登録者

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. (登録日: 2005-08-01, 公開日: 2006-02-22, 最終更新日: 2024-06-19)

主引用文献

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

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: 16483931
DOI: 10.1016/J.MOLCEL.2006.01.008

実験手法

SOLUTION NMR