3tkn | pdb_00003tkn

Structure of the Nup82-Nup159-Nup98 heterotrimer

spinqualitylabelsall models 3tkn, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tkn is a 9 chain structure with sequence from Mus musculus and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: HRB187, J1135, NUP82, YJL061W (Saccharomyces cerevisiae), NUP158, NUP159, RAT7, YIL115C (Saccharomyces cerevisiae), Nup98 (Mus musculus) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NUP82_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. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain. [Q6PFD9_MOUSE] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC (By similarity). [NU159_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). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export. Publication Abstract from PubMed The cytoplasmic filament nucleoporins of the nuclear pore complex (NPC) are critically involved in nuclear export and remodeling of mRNA ribonucleoprotein particles and are associated with various human malignancies. Here, we report the crystal structure of the Nup98 C-terminal autoproteolytic domain, frequently missing from leukemogenic forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 beta propeller serves as a noncooperative binding platform for both binding partners. Interaction of Nup98 with Nup82 occurs through a reciprocal exchange of loop structures. Strikingly, the same Nup98 groove promiscuously interacts with Nup82 and Nup96 in a mutually excusive fashion. Simultaneous disruption of both Nup82 interactions in yeast causes severe defects in mRNA export, while the severing of a single interaction is tolerated. Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport. Molecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore Complex.,Stuwe TT, von Borzyskowski LS, Davenport AM, Hoelz A J Mol Biol. 2012 Apr 2. PMID:22480613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoporin

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