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The 2.0 A crystal structure of a heterotrimeric G protein
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scholarly article
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title
The 2.0 A crystal structure of a heterotrimeric G protein
(English)
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main subject
crystal structure
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protein structure
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author name string
D G Lambright
series ordinal
1
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J Sondek
series ordinal
2
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A Bohm
series ordinal
3
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N P Skiba
series ordinal
4
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H E Hamm
series ordinal
5
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P B Sigler
series ordinal
6
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language of work or name
English
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publication date
25 January 1996
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published in
Nature
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volume
379
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page(s)
311-9
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issue
6563
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cites work
Structural elements of G alpha subunits that interact with G beta gamma, receptors, and effectors
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Heterotrimeric G proteins: organizers of transmembrane signals
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Diversity of G proteins in signal transduction
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G proteins
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Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits.
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Signal transduction enzymes of vertebrate photoreceptors
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Interactions of a G-protein with its effector: transducin and cGMP phosphodiesterase in retinal rods
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Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
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The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
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GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4
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Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
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Mapping of effector binding sites of transducin alpha-subunit using G alpha t/G alpha i1 chimeras
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Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis
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The ancient regulatory-protein family of WD-repeat proteins
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Effect of monoclonal antibody binding on alpha-beta gamma subunit interactions in the rod outer segment G protein, Gt
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A mutation that prevents GTP-dependent activation of the alpha chain of Gs.
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Intersubunit surfaces in G protein alpha beta gamma heterotrimers. Analysis by cross-linking and mutagenesis of beta gamma
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Genetic identification of residues involved in association of alpha and beta G-protein subunits
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Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
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Farnesylated γ-subunit of photoreceptor G protein indispensable for GTP-binding
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The gamma subunit of transducin is farnesylated
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G protein gamma subunits contain a 20-carbon isoprenoid
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Brain G protein gamma subunits contain an all-trans-geranylgeranylcysteine methyl ester at their carboxyl termini
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Myristoylated alpha subunits of guanine nucleotide-binding regulatory proteins
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Lipid modification at the N terminus of photoreceptor G-protein alpha-subunit
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Lipid modifications of G proteins: alpha subunits are palmitoylated
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Activation and depalmitoylation of Gs alpha
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Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding
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Identification of receptor contact site involved in receptor-G protein coupling.
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The carboxyl terminus of Scg1, the G alpha subunit involved in yeast mating, is implicated in interactions with the pheromone receptors.
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Gi2 mediates alpha 2-adrenergic inhibition of adenylyl cyclase in platelet membranes: in situ identification with G alpha C-terminal antibodies
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Substitution of three amino acids switches receptor specificity of Gq alpha to that of Gi alpha
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Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit
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NMR structure of a receptor-bound G-protein peptide
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50 Transducin and the cyclic GMP phosphodiesterase of retinal rod outer segments
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Biochemical and genetic analysis of dominant-negative mutations affecting a yeast G-protein gamma subunit
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Identifiers
DOI
10.1038/379311A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1611907
Dimensions Publication ID
1048752425
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OpenCitations bibliographic resource ID
1611907
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1611907
PubMed ID
8552184
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1611907
ResearchGate publication ID
14648710
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Springer Nature article ID
10.1038/379311a0
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