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  Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form

Scheffzek, K., Klebe, C., Fritz-Wolf, K., Kabsch, W., & Wittinghofer, A. (1995). Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature, 374(6520), 378-381. doi:10.1038/374378a0.

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Genre: Journal Article
Alternative Title : Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form

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Nature_374_1995_378.pdf (Any fulltext), 449KB
 
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 Creators:
Scheffzek, Klaus1, Author           
Klebe, Christian, Author
Fritz-Wolf, Karin1, 2, Author           
Kabsch, Wolfgang1, 2, 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              

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 Abstract: THE Ran proteins constitute a distinct branch of the superfamily of Ras-related GTP-binding proteins which function as molecular switches cycling between GTP-bound 'on' and GDP-bound 'off' states. Ran is located predominantly in the nucleus of eukaryotic cells and is involved in the nuclear import of proteins as well as in control of DNA synthesis and of cell-cycle progression. We report here the crystal structure at 2.3 Å resolution of human Ran (Mr 24K) complexed with GDP and Mg2+. This structure reveals a similarity with the Ras core (G-domain) but with significant variations in regions involved in GDP and Mg2+ coordination (switch I and switch II regions in Ras)9,10, suggesting that there could be major conformational changes upon GTP binding. In addition to the G-domain, an extended chain and an alpha-helix were identified at the carboxy terminus. The amino-terminal (amino-acid residues MAAQGEP) stretch and the acidic tail (211DEDDDL216) appear to be flexible in the crystal structure.

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Language(s): eng - English
 Dates: 1994-11-071995-01-311995-03-23
 Publication Status: Issued
 Pages: 4
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 Rev. Type: Peer
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 374 (6520) Sequence Number: - Start / End Page: 378 - 381 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238