Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5TDH

The crystal structure of the dominant negative mutant G protein alpha(i)-1-beta-1-gamma-2 G203A/A326S

Summary for 5TDH
Entry DOI10.2210/pdb5tdh/pdb
DescriptorGuanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (4 entities in total)
Functional Keywordsdominant negative, g-alpha(i)-1-beta-1-gamma-2 heterotrimer, g203a, a326s, gpcr, gdp, cell cycle
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus : P63096
Cell membrane ; Lipid-anchor ; Cytoplasmic side : P63212
Total number of polymer chains6
Total formula weight172022.18
Authors
Liu, P.,Jia, M.-Z.,Zhou, X.E.,de Waal, P.W.,Dickson, B.M.,Liu, B.,Hou, L.,Yin, Y.-T.,Kang, Y.-Y.,Shi, Y.,Melcher, K.,Xu, H.E.,Jiang, Y. (deposition date: 2016-09-19, release date: 2016-11-09, Last modification date: 2024-03-20)
Primary citationLiu, P.,Jia, M.-Z.,Zhou, X.E.,De Waal, P.W.,Dickson, B.M.,Liu, B.,Hou, L.,Yin, Y.-T.,Kang, Y.-Y.,Shi, Y.,Melcher, K.,Xu, H.E.,Jiang, Y.
The structural basis of the dominant negative phenotype of the G alpha i1 beta 1 gamma 2 G203A/A326S heterotrimer
Acta Pharmacol.Sin., 37:1259-1272, 2016
Cited by
PubMed Abstract: Dominant negative mutant G proteins have provided critical insight into the mechanisms of G protein-coupled receptor (GPCR) signaling, but the mechanisms underlying the dominant negative characteristics are not completely understood. The aim of this study was to determine the structure of the dominant negative Gαi1β1γ2 G203A/A326S complex (Gi-DN) and to reveal the structural basis of the mutation-induced phenotype of Gαi1β1γ2.
PubMed: 27498775
DOI: 10.1038/aps.2016.69
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

237735

건을2025-06-18부터공개중

PDB statisticsPDBj update infoContact PDBjnumon