2MSE
NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc
Summary for 2MSE
Entry DOI | 10.2210/pdb2mse/pdb |
Related | 1AV1 2M4A 2M4B 2MSC 2MSD 3GFT 4DSN |
NMR Information | BMRB: 25116 |
Descriptor | Apolipoprotein A-I, GTPase KRas, Serine/threonine-protein kinase A-Raf, ... (7 entities in total) |
Functional Keywords | k-ras, nanodisc, pre, docking, a-rafrbd, lipid binding protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 139393.26 |
Authors | Mazhab-Jafari, M.,Stathopoulos, P.,Marshall, C.,Ikura, M. (deposition date: 2014-07-29, release date: 2015-06-03, Last modification date: 2019-12-11) |
Primary citation | Mazhab-Jafari, M.T.,Marshall, C.B.,Smith, M.J.,Gasmi-Seabrook, G.M.,Stathopulos, P.B.,Inagaki, F.,Kay, L.E.,Neel, B.G.,Ikura, M. Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112:6625-6630, 2015 Cited by PubMed: 25941399DOI: 10.1073/pnas.1419895112 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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