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  Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

Pai, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J. J., & Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature, 341(6239), 209-214. doi:10.1038/341209a0.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AD91-2 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-8531-2
Genre: Journal Article

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Nature_341_1989_209.pdf (Any fulltext), 739KB
 
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Pai, Emil F., Author
Kabsch, Wolfgang1, 2, Author           
Krengel, Ute1, Author           
Holmes, Kenneth C.1, 3, 4, Author           
John, Jacob J., Author
Wittinghofer, Alfred1, 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              
3Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society, ou_1497735              
4Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              

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 Abstract: The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5'-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. The topological order of secondary structure elements is the same as that of the guanine-nucleotide-binding domain of bacterial elongation factor EF-Tu. Many interactions between nucleotide and protein have been identified. The effects of point mutations and the conservation of amino-acid sequence in the guanine-nucleotide-binding proteins are discussed.

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Language(s): eng - English
 Dates: 1989-07-111989-08-251989-09-21
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/341209a0
URI: https://www.ncbi.nlm.nih.gov/pubmed/2476675
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 341 (6239) Sequence Number: - Start / End Page: 209 - 214 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238