3ch5 | pdb_00003ch5

The crystal structure of the RanGDP-Nup153ZnF2 complex

spinqualitylabelsall models 3ch5, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ch5 is a 2 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, MG, SO4, ZN Related: 2koc, 2ebv, 2gqe, 2ebq, 2ebr, 1ibr Gene: RAN, ARA24 (HUMAN), Nup153 (Buffalo rat) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [RAN_HUMAN] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases. [NU153_RAT] Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. 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 Nucleoporin (Nup) 153 is a highly mobile, multifunctional, and essential nuclear pore protein. It contains four zinc finger motifs that are thought to be crucial for the regulation of transport-receptor/cargo interactions via their binding to the small guanine nucleotide binding protein, Ran. We found this interaction to be independent of the phoshorylation state of the nucleotide. Ran binds with the highest affinity to the second zinc finger motif of Nup153 (Nup153ZnF2). Here we present the crystal structure of this complex, revealing a new type of Ran-Ran interaction partner interface together with the solution structure of Nup153ZnF2. According to our complex structure, Nup153ZnF2 binding to Ran excludes the formation of a Ran-importin-beta complex. This finding suggests a local Nup153-mediated Ran reservoir at the nucleoplasmic distal ring of the nuclear pore, where nucleotide exchange may take place in a ternary Nup153-Ran-RCC1 complex, so that import complexes are efficiently terminated. The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex.,Schrader N, Koerner C, Koessmeier K, Bangert JA, Wittinghofer A, Stoll R, Vetter IR Structure. 2008 Jul;16(7):1116-25. PMID:18611384 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GTP-binding protein Nucleoporin

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