1gy5
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D92N,D94N DOUBLE POINT MUTANT OF HUMAN NUCLEAR TRANSPORT FACTOR 2 (NTF2)
OverviewOverview
Interactions with nucleoporins containing FxFG-repeat cores are crucial, for the nuclear import of RanGDP mediated by nuclear transport factor 2, (NTF2). We describe here the 1.9 A resolution crystal structure of yeast, NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for, understanding this interaction and its role in nuclear trafficking. The, two identical FxFG binding sites on the dimeric molecule are formed by, residues from each chain of NTF2. Engineered mutants at the interaction, interface reduce the binding of NTF2 to nuclear pores and cause reduced, growth rates and Ran mislocalization when substituted for the wild-type, protein in yeast. Comparison with the crystal structure of FG-nucleoporin, cores bound to importin-beta and TAP/p15 identified a number of common, features of their binding sites. The structure of the binding interfaces, on these transport factors provides a rationale for the specificity of, their interactions with nucleoporins that, combined with their weak, binding constants, facilitates rapid translocation through NPCs during, nuclear trafficking.
About this StructureAbout this Structure
1GY5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats., Bayliss R, Leung SW, Baker RP, Quimby BB, Corbett AH, Stewart M, EMBO J. 2002 Jun 17;21(12):2843-53. PMID:12065398
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