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

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...

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Detalles Bibliográficos
Autores principales: Wittinghofer, F, Krengel, U, John, J, Kabsch, W, Pai, E F
Formato: Texto
Lenguaje:English
Publicado: 1991
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568068/
https://www.ncbi.nlm.nih.gov/pubmed/1773783
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author Wittinghofer, F
Krengel, U
John, J
Kabsch, W
Pai, E F
author_facet Wittinghofer, F
Krengel, U
John, J
Kabsch, W
Pai, E F
author_sort Wittinghofer, F
collection PubMed
description 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 has been analyzed in detail. It shows that the overall structure of the mutant is not perturbed and that the side chain of Arg12 is coming close to the gamma-phosphate for an interaction.
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spelling pubmed-15680682006-09-18 Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant. Wittinghofer, F Krengel, U John, J Kabsch, W Pai, E F Environ Health Perspect Research Article 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 has been analyzed in detail. It shows that the overall structure of the mutant is not perturbed and that the side chain of Arg12 is coming close to the gamma-phosphate for an interaction. 1991-06 /pmc/articles/PMC1568068/ /pubmed/1773783 Text en
spellingShingle Research Article
Wittinghofer, F
Krengel, U
John, J
Kabsch, W
Pai, E F
Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title_full Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title_fullStr Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title_full_unstemmed Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title_short Three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
title_sort three-dimensional structure of p21 in the active conformation and analysis of an oncogenic mutant.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568068/
https://www.ncbi.nlm.nih.gov/pubmed/1773783
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