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

doi:10.1289/ehp.919311

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Article

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

Environmental health perspectives - 1 Jun 1991

Wittinghofer F, Krengel U, John J, Kabsch W, Pai E F

Abstract excerpt

The three-dimensional structure of the active guanosine triphosphate (GTP)-analogue-containing complex of the H-ras-encoded p21 has been determined. It was necessary to correct the topology of p21 as published earlier. The structure analysis shows all of the interactions between protein and GTP and how the important cofactor Mg2+ is bound. From the oncogenic mutants of p21 crystallized, a Gly12 to Arg mutation...

Topics

Allosteric Regulation
Amino Acid Sequence
Binding Sites
Enzyme Activation
GTP Phosphohydrolases
GTPase-Activating Proteins
Guanosine Diphosphate
Guanosine Triphosphate
Humans
Hydrogen Bonding
Magnesium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Molecular Structure

Mutation

Protein Binding

Protein Conformation

Proteins

Source

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Identifiers

PMID: 1773783
DOI: 10.1289/ehp.919311
PMCID: PMC1568068

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1773783-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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