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  Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

Rak, A., Pylypenko, O., Durek, T., Watzke, A., Kushnir, S., Brunsveld, L., et al. (2003). Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science, 302(5645), 646-650. doi:10.1126/science.1087761.

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Genre: Journal Article
Alternative Title : Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

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Science_302_2003_646.pdf (Any fulltext), 571KB
 
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Rak, Alexey, Author
Pylypenko, Olena1, Author           
Durek, Thomas, Author
Watzke, Anja, Author
Kushnir, Susanna, Author
Brunsveld, Lucas, Author
Waldmann, Herbert, Author
Goody, Roger S.2, Author           
Alexandrov, Kirill, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.

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Language(s): eng - English
 Dates: 2003-06-092003-09-052003-10-24
 Publication Status: Published in print
 Pages: 34
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 Rev. Type: Peer
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 302 (5645) Sequence Number: - Start / End Page: 646 - 650 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1