2C5L

Structure of PLC epsilon Ras association domain with hRas

Summary for 2C5L

• Entry DOI: 10.2210/pdb2c5l/pdb
• 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
• Descriptor: GTPASE HRAS, PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C PLC-EPSILON, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: signaling protein-complex, ras, ubiquitin superfold, oncogene, gtp-binding, nucleotide- binding, signaling protein, disease mutation, lipoprotein, palmitate, prenylation, proto-oncogene
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cell membrane. Isoform 2: Nucleus: P01112
• Total number of polymer chains: 4
• Total formula weight: 66532.44

Authors

Roe, S.M.,Bunney, T.D.,Katan, M.,Pearl, L.H. (deposition date: 2005-10-27, release date: 2006-02-20, Last modification date: 2024-05-08)

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.,Gieschik, 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

Experimental method

X-RAY DIFFRACTION (1.9 Å)