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2MSC

NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc

Summary for 2MSC
Entry DOI10.2210/pdb2msc/pdb
Related1AV1 2M4A 2M4B 2MSD 2MSE 3GFT 4DSN
NMR InformationBMRB: 25114
DescriptorApolipoprotein A-I, GTPase KRas, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (6 entities in total)
Functional Keywordsk-ras, nanodisc, pre, docking, lipid binding protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight131180.78
Authors
Mazhab-Jafari, M.,Stathopoulos, P.,Marshall, C.,Ikura, M. (deposition date: 2014-07-29, release date: 2015-06-03, Last modification date: 2024-05-01)
Primary citationMazhab-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: 25941399
DOI: 10.1073/pnas.1419895112
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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