2aiv | pdb_00002aiv

Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116P

spinqualitylabelsall models 2aiv, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2aiv is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: NUP116, NSP116 (ATCC 18824) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NU116_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The yeast nucleoporin Nup116p plays an important role in mRNA export and protein transport. We have determined the solution structure of the C-terminal 147 residues of this protein, the region responsible for targeting the protein to the nuclear pore complex (NPC). The structure of Nup116p-C consists of a large beta-sheet sandwiched against a smaller one, flanked on both sides by alpha-helical stretches, similar to the structure of its human homolog, NUP98. In unliganded form, Nup116p-C exhibits evidence of exchange among multiple conformations, raising the intriguing possibility that it may adopt distinct conformations when bound to different partners in the NPC. We have additionally shown that a peptide from the N terminus of the nucleoporin Nup145p-C binds Nup116p-C. This previously unknown interaction may explain the unusual asymmetric localization pattern of Nup116p in the NPC. Strikingly, the exchange phenomenon observed in the unbound state is greatly reduced in the corresponding spectra of peptide-bound Nup116p-C, suggesting that the binding interaction stabilizes the domain conformation. This study offers a high resolution view of a yeast nucleoporin structural domain and may provide insights into NPC architecture and function. Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p.,Robinson MA, Park S, Sun ZY, Silver PA, Wagner G, Hogle JM J Biol Chem. 2005 Oct 21;280(42):35723-32. Epub 2005 Aug 16. PMID:16105837 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoporin 3D structures

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