3ran: Difference between revisions
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'''CANINE GDP-RAN Q69L MUTANT''' | '''CANINE GDP-RAN Q69L MUTANT''' | ||
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[[Category: Mccoy, A J.]] | [[Category: Mccoy, A J.]] | ||
[[Category: Stewart, M.]] | [[Category: Stewart, M.]] | ||
[[Category: | [[Category: Gtpase]] | ||
[[Category: | [[Category: Nuclear transport]] | ||
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Revision as of 22:11, 4 May 2008
CANINE GDP-RAN Q69L MUTANT
OverviewOverview
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.
About this StructureAbout this Structure
3RAN is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sun May 4 22:11:47 2008