3ran

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{{STRUCTURE_3ran| PDB=3ran | SCENE= }}
{{STRUCTURE_3ran| PDB=3ran | SCENE= }}
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'''CANINE GDP-RAN Q69L MUTANT'''
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===CANINE GDP-RAN Q69L MUTANT===
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==Overview==
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We report the 2.3 A resolution X-ray crystal structure of the GDP-bound form of the RanQ69L mutant that is used extensively in studies of nucleocytoplasmic transport and cell-cycle progression. When the structure of GDP-RanQ69L from monoclinic crystals with P21 symmetry was compared with the structure of wild-type Ran obtained from monoclinic crystals, the Q69L mutant showed a large conformational change in residues 68-74, which are in the switch II region of the molecule which changes conformation in response to nucleotide state and which forms the major interaction interface with nuclear transport factor 2 (NTF2, sometimes called p10). This conformational change alters the positions of key residues such as Lys71, Phe72 and Arg76 that are crucial for the interaction of GDP-Ran with NTF2 and indeed, solution binding studies were unable to detect any interaction between NTF2 and GDP-RanQ69L under conditions where GDP-Ran bound effectively. This interaction between NTF2 and GDP-Ran is required for efficient nuclear protein import and may function between the docking and translocation steps of the pathway.
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==About this Structure==
==About this Structure==
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[[Category: Gtpase]]
[[Category: Gtpase]]
[[Category: Nuclear transport]]
[[Category: Nuclear transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:04:45 2008''

Revision as of 10:04, 3 July 2008

Image:3ran.png

Template:STRUCTURE 3ran

CANINE GDP-RAN Q69L MUTANT

Template:ABSTRACT PUBMED 9878368

About this Structure

3RAN is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

Reference

The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2)., Stewart M, Kent HM, McCoy AJ, J Mol Biol. 1998 Dec 18;284(5):1517-27. PMID:9878368

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