1GYB
N77Y point mutant of yNTF2 bound to FxFG nucleoporin repeat
Summary for 1GYB
Entry DOI | 10.2210/pdb1gyb/pdb |
Related | 1GY5 1GY6 1GY7 |
Descriptor | NUCLEAR TRANSPORT FACTOR 2, NUCLEOPORIN (3 entities in total) |
Functional Keywords | nuclear transport |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Cellular location | Cytoplasm: P33331 |
Total number of polymer chains | 8 |
Total formula weight | 61776.27 |
Authors | Bayliss, R.,Stewart, M. (deposition date: 2002-04-22, release date: 2002-06-20, Last modification date: 2024-05-08) |
Primary citation | Bayliss, R.,Leung, S.,Baker, R.,Quimby, B.,Corbett, A.,Stewart, M. Structural Basis for the Interaction between Ntf2 and Nucleoporin Fxfg Repeats Embo J., 21:2843-, 2002 Cited by PubMed Abstract: 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. PubMed: 12065398DOI: 10.1093/EMBOJ/CDF305 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
