2MSD
NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc
Summary for 2MSD
Entry DOI | 10.2210/pdb2msd/pdb |
Related | 1AV1 2M4A 2M4B 2MSC 2MSE 3GFT 4DSN |
NMR Information | BMRB: 25115 |
Descriptor | Apolipoprotein A-I, GTPase KRas, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (6 entities in total) |
Functional Keywords | k-ras, nanodisc, pre, docking, lipid binding protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 131259.77 |
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 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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