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Ras/Rap effector specificity determined by charge reversal

Members of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we... Full description

Journal Title: Nature structural & molecular biology 1996-08, Vol.3 (8), p.723-729
Main Author: Nassar, Nicolas
Other Authors: Horn, Gudrun , Herrmann, Christian , Block, Christoph , Janknecht, Ralf , Wittinghofer, Alfred
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States
ID: ISSN: 1072-8368
Link: https://www.ncbi.nlm.nih.gov/pubmed/8756332
Zum Text:
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recordid: cdi_proquest_miscellaneous_78195618
title: Ras/Rap effector specificity determined by charge reversal
format: Article
creator:
  • Nassar, Nicolas
  • Horn, Gudrun
  • Herrmann, Christian
  • Block, Christoph
  • Janknecht, Ralf
  • Wittinghofer, Alfred
subjects:
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Genes, Reporter
  • GTP-Binding Proteins - chemistry
  • GTP-Binding Proteins - genetics
  • GTP-Binding Proteins - metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding - genetics
  • Protein-Serine-Threonine Kinases - chemistry
  • Protein-Serine-Threonine Kinases - genetics
  • Protein-Serine-Threonine Kinases - metabolism
  • Proto-Oncogene Proteins - chemistry
  • Proto-Oncogene Proteins - genetics
  • Proto-Oncogene Proteins - metabolism
  • Proto-Oncogene Proteins c-raf
  • Rabbits
  • rap GTP-Binding Proteins
  • ras Proteins - chemistry
  • ras Proteins - genetics
  • ras Proteins - metabolism
  • Structure-Activity Relationship
  • Transcriptional Activation
  • Transfection
ispartof: Nature structural & molecular biology, 1996-08, Vol.3 (8), p.723-729
description: Members of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we have introduced the mutations E30D and K31E into Rap and show biochemically, by X-ray structure analysis and by transfection in vivo that the identical core effector region of Ras and Rap (residues 32-40) is responsible for molecular recognition, but that residues outside this region are responsible for the specificity of the interaction. The major determinant for the switch in specificity is the opposite charge of residue 31--Lys in Rap, Glu in Ras--which creates a favourable complementary interface for the Ras-Raf interaction.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 1072-8368
fulltext: fulltext
issn:
  • 1072-8368
  • 1545-9993
  • 2331-365X
  • 1545-9985
url: Link


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creatorNassar, Nicolas ; Horn, Gudrun ; Herrmann, Christian ; Block, Christoph ; Janknecht, Ralf ; Wittinghofer, Alfred
creatorcontribNassar, Nicolas ; Horn, Gudrun ; Herrmann, Christian ; Block, Christoph ; Janknecht, Ralf ; Wittinghofer, Alfred
descriptionMembers of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we have introduced the mutations E30D and K31E into Rap and show biochemically, by X-ray structure analysis and by transfection in vivo that the identical core effector region of Ras and Rap (residues 32-40) is responsible for molecular recognition, but that residues outside this region are responsible for the specificity of the interaction. The major determinant for the switch in specificity is the opposite charge of residue 31--Lys in Rap, Glu in Ras--which creates a favourable complementary interface for the Ras-Raf interaction.
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subjectAmino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallography, X-Ray ; Genes, Reporter ; GTP-Binding Proteins - chemistry ; GTP-Binding Proteins - genetics ; GTP-Binding Proteins - metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Binding - genetics ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proto-Oncogene Proteins - chemistry ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-raf ; Rabbits ; rap GTP-Binding Proteins ; ras Proteins - chemistry ; ras Proteins - genetics ; ras Proteins - metabolism ; Structure-Activity Relationship ; Transcriptional Activation ; Transfection
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descriptionMembers of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we have introduced the mutations E30D and K31E into Rap and show biochemically, by X-ray structure analysis and by transfection in vivo that the identical core effector region of Ras and Rap (residues 32-40) is responsible for molecular recognition, but that residues outside this region are responsible for the specificity of the interaction. The major determinant for the switch in specificity is the opposite charge of residue 31--Lys in Rap, Glu in Ras--which creates a favourable complementary interface for the Ras-Raf interaction.
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13Protein-Serine-Threonine Kinases - chemistry
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abstractMembers of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we have introduced the mutations E30D and K31E into Rap and show biochemically, by X-ray structure analysis and by transfection in vivo that the identical core effector region of Ras and Rap (residues 32-40) is responsible for molecular recognition, but that residues outside this region are responsible for the specificity of the interaction. The major determinant for the switch in specificity is the opposite charge of residue 31--Lys in Rap, Glu in Ras--which creates a favourable complementary interface for the Ras-Raf interaction.
copUnited States
pmid8756332
doi10.1038/nsb0896-723