1ukv: Difference between revisions

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[[Image:1ukv.gif|left|200px]]
{{Seed}}
[[Image:1ukv.png|left|200px]]


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{{STRUCTURE_1ukv|  PDB=1ukv  |  SCENE=  }}  
{{STRUCTURE_1ukv|  PDB=1ukv  |  SCENE=  }}  


'''Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase'''
===Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase===




==Overview==
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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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{{ABSTRACT_PUBMED_14576435}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Vesicular transport]]
[[Category: Vesicular transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:56:42 2008''

Revision as of 00:56, 28 July 2008

File:1ukv.png

Template:STRUCTURE 1ukv

Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

Template:ABSTRACT PUBMED 14576435

About this Structure

1UKV is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase., Rak A, Pylypenko O, Durek T, Watzke A, Kushnir S, Brunsveld L, Waldmann H, Goody RS, Alexandrov K, Science. 2003 Oct 24;302(5645):646-50. PMID:14576435

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