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  The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast

Scheffzek, K., Grünewald, P., Wohlgemuth, S., Kabsch, W., Tu, H., Wigler, M., et al. (2001). The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast. Structure, 9(11), 1043-1050. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11709168.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-1F19-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-1F1A-C
Genre: Journal Article
Alternative Title : The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast

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 Creators:
Scheffzek, Klaus1, Author              
Grünewald, Petra, Author
Wohlgemuth, Sabine, Author
Kabsch, Wolfgang1, 2, Author              
Tu, Hua, Author
Wigler, Mike, Author
Wittinghofer, Alfred1, Author              
Herrmann, Christine, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Byr2-kinase; mutational analysis; Schizosaccharomyces pombe; Ras signaling; GTP binding protein, cancer; GTPase; X-ray crystallography
 Abstract: BACKGROUND: The small GTP binding protein Ras has important roles in cellular growth and differentiation. Mutant Ras is permanently active and contributes to cancer development. In its activated form, Ras interacts with effector proteins, frequently initiating a kinase cascade. In the lower eukaryotic Schizosaccharomyces pombe, Byr2 kinase represents a Ras target that in terms of signal-transduction hierarchy can be considered a homolog of mammalian Raf-kinase. The activation mechanism of protein kinases by Ras is not understood, and there is no detailed structural information about Ras binding domains (RBDs) in nonmammalian organisms. RESULTS: The crystal structure of the Ras-Byr2RBD complex at 3 A resolution shows a complex architecture similar to that observed in mammalian homologous systems, with an interprotein beta sheet stabilized by predominantly polar interactions between the interacting components. The C-terminal half of the Ras switch I region contains most of the contact anchors, while on the Byr2 side, a number of residues from topologically distinct regions are involved in complex stabilization. A C-terminal helical segment, which is not present in the known mammalian homologous systems and which is part of the auto-inhibitory region, has an additional binding site outside the switch I region. CONCLUSIONS: The structure of the Ras-Byr2 complex confirms the Ras binding module as a communication element mediating Ras-effector interactions; the Ras-Byr2 complex is also conserved in a lower eukaryotic system like yeast, which is in contrast to other small GTPase families. The extra helical segment might be involved in kinase activation.

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Language(s): eng - English
 Dates: 2001-08-172001-10-172001-11-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 9 (11) Sequence Number: - Start / End Page: 1043 - 1050 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1