3nby: Difference between revisions

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-[[Image:3nby.png|left|200px]]
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-The line below this paragraph, containing "STRUCTURE_3nby", creates the "Structure Box" on the page.
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 {{STRUCTURE_3nby|  PDB=3nby  |  SCENE=  }}
 ===Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex===
+{{ABSTRACT_PUBMED_20972448}}
+==Function==
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+[[http://www.uniprot.org/uniprot/SPN1_HUMAN SPN1_HUMAN]] Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs.<ref>PMID:9670026</ref>  [[http://www.uniprot.org/uniprot/XPO1_MOUSE XPO1_MOUSE]] Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity).<ref>PMID:20921223</ref>  [[http://www.uniprot.org/uniprot/RAN_HUMAN 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.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>   Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
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-{{ABSTRACT_PUBMED_20972448}}
 ==About this Structure==
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 ==Reference==
-<ref group="xtra">PMID:20972448</ref><references group="xtra"/>
+<ref group="xtra">PMID:020972448</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Mus musculus]]
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 [[Category: Neumann, P.]]
 [[Category: Sattler, M.]]
+[[Category: Gtp-binding protein-transport protein complex]]
+[[Category: Protein transport]]