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Article

Three-dimensional structure of p21H-ras and its implications.

Seminars in cancer biology - 1 Aug 1992

Wittinghofer F

Abstract excerpt

The three-dimensional structure of the H-ras oncogene product p21 has been determined in both its active, GTP-bound and its inactive, GDP-bound forms. This has supplied a wealth of information on the mode of binding of guanine nucleotides, on the mechanism of the GTPase reaction and on the conformational change of the protein which accompanies GTP hydrolysis. The structural analysis has also given clues to the...

Topics

Amino Acid Sequence
Animals
Binding Sites
GTPase-Activating Proteins
Guanosine Triphosphate
Humans
Hydrolysis
Molecular Conformation
Molecular Sequence Data
Mutation
Proteins
Proto-Oncogene Proteins p21(ras)

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

ras GTPase-Activating Proteins

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Identifiers

PMID: 1421163

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1421163-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Three-dimensional structure of p21H-ras and its implications.PMID 1421163Read ↗

Three-dimensional structure and properties of wild-type and mutant H-ras-encoded p21.Semantic proximity Read ↗

Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.Semantic proximity Read ↗

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Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules.Semantic proximity Read ↗

K-Ras Populates Conformational States Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D.Semantic proximity Read ↗

Activated conformations of the ras-gene-encoded p21 protein. 2. Comparison of the computed and high-resolution x-ray crystallographic structures of Gly-12 p21.Semantic proximity Read ↗

X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.Semantic proximity Read ↗

Proton NMR studies of transforming and nontransforming H-ras p21 mutants.Semantic proximity Read ↗

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Comparison of the low energy conformations of an oncogenic and a non-oncogenic p21 protein, neither of which binds GTP or GDP.Semantic proximity Read ↗

p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.Semantic proximity Read ↗

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