3nc1

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{{STRUCTURE_3nc1| PDB=3nc1 | SCENE= }}
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==Crystal structure of the CRM1-RanGTP complex==
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===Crystal structure of the CRM1-RanGTP complex===
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<StructureSection load='3nc1' size='340' side='right' caption='[[3nc1]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
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{{ABSTRACT_PUBMED_20972448}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3nc1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NC1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARA24, OK/SW-cl.81, RAN, RAN (GeneID: 5901) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Crm1, Xpo1, Xpo1 (GeneID: 103573) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nc1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nc1 RCSB], [http://www.ebi.ac.uk/pdbsum/3nc1 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP-CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Phi) residues, yet CRM1 recognizes them with the same rigid set of five Phi pockets. The different Phi spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an alpha-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Phi pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly.
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==Function==
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NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.,Guttler T, Madl T, Neumann P, Deichsel D, Corsini L, Monecke T, Ficner R, Sattler M, Gorlich D Nat Struct Mol Biol. 2010 Oct 24. PMID:20972448<ref>PMID:20972448</ref>
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[[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> [[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>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3nc1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NC1 OCA].
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:020972448</ref><references group="xtra"/><references/>
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*[[Exportin|Exportin]]
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*[[GTP-binding protein|GTP-binding protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Corsini, L.]]
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[[Category: Corsini, L]]
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[[Category: Deichsel, D.]]
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[[Category: Deichsel, D]]
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[[Category: Ficner, R.]]
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[[Category: Ficner, R]]
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[[Category: Gorlich, D.]]
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[[Category: Gorlich, D]]
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[[Category: Guttler, T.]]
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[[Category: Guttler, T]]
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[[Category: Madl, T.]]
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[[Category: Madl, T]]
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[[Category: Monecke, T.]]
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[[Category: Monecke, T]]
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[[Category: Neumann, P.]]
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[[Category: Neumann, P]]
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[[Category: Sattler, M.]]
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[[Category: Sattler, M]]
[[Category: Gtp-binding protein-transport protein complex]]
[[Category: Gtp-binding protein-transport protein complex]]
[[Category: Protein transport]]
[[Category: Protein transport]]

Revision as of 16:28, 18 December 2014

Crystal structure of the CRM1-RanGTP complex

3nc1, resolution 3.35Å

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