1w9c

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[[Image:1w9c.jpg|left|200px]]
 
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==Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats==
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The line below this paragraph, containing "STRUCTURE_1w9c", creates the "Structure Box" on the page.
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<StructureSection load='1w9c' size='340' side='right'caption='[[1w9c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W9C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w9c OCA], [https://pdbe.org/1w9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w9c RCSB], [https://www.ebi.ac.uk/pdbsum/1w9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w9c ProSAT]</span></td></tr>
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{{STRUCTURE_1w9c| PDB=1w9c | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XPO1_HUMAN XPO1_HUMAN] 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 (Ran-GTP). 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. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.<ref>PMID:9323133</ref> <ref>PMID:9311922</ref> <ref>PMID:9837918</ref> <ref>PMID:14612415</ref> <ref>PMID:15574332</ref> <ref>PMID:20921223</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w9/1w9c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w9c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CRM1/Exportin1 mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES) by forming a cooperative ternary complex with the NES-bearing substrate and the small GTPase Ran. We present a structural model of human CRM1 based on a combination of X-ray crystallography, homology modeling, and electron microscopy. The architecture of CRM1 resembles that of the import receptor transportin1, with 19 HEAT repeats and a large loop implicated in Ran binding. Residues critical for NES recognition are identified adjacent to the cysteine residue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. We present evidence that a conformational change of the Ran binding loop accounts for the cooperativity of Ran- and substrate binding and for the selective enhancement of CRM1-mediated export by the cofactor RanBP3. Our findings indicate that a single architectural and mechanistic framework can explain the divergent effects of RanGTP on substrate binding by many import and export receptors.
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'''PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS'''
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Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.,Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW Mol Cell. 2004 Dec 3;16(5):761-75. PMID:15574331<ref>PMID:15574331</ref>
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==Overview==
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CRM1/Exportin1 mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES) by forming a cooperative ternary complex with the NES-bearing substrate and the small GTPase Ran. We present a structural model of human CRM1 based on a combination of X-ray crystallography, homology modeling, and electron microscopy. The architecture of CRM1 resembles that of the import receptor transportin1, with 19 HEAT repeats and a large loop implicated in Ran binding. Residues critical for NES recognition are identified adjacent to the cysteine residue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. We present evidence that a conformational change of the Ran binding loop accounts for the cooperativity of Ran- and substrate binding and for the selective enhancement of CRM1-mediated export by the cofactor RanBP3. Our findings indicate that a single architectural and mechanistic framework can explain the divergent effects of RanGTP on substrate binding by many import and export receptors.
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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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1W9C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9C OCA].
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</div>
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<div class="pdbe-citations 1w9c" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex., Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW, Mol Cell. 2004 Dec 3;16(5):761-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15574331 15574331]
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*[[Exportin 3D structures|Exportin 3D structures]]
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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]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Askjaer, P.]]
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[[Category: Askjaer P]]
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[[Category: Baudin, F.]]
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[[Category: Baudin F]]
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[[Category: Bauer, U.]]
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[[Category: Bauer U]]
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[[Category: Mattaj, I W.]]
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[[Category: Mattaj IW]]
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[[Category: Moulin, M.]]
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[[Category: Moulin M]]
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[[Category: Muller, C W.]]
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[[Category: Muller CW]]
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[[Category: Petosa, C.]]
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[[Category: Petosa C]]
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[[Category: Schoehn, G.]]
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[[Category: Schoehn G]]
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[[Category: Soler-Lopez, M.]]
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[[Category: Soler-Lopez M]]
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[[Category: Steuerwald, U.]]
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[[Category: Steuerwald U]]
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[[Category: Exportin 1]]
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[[Category: Nuclear export complex]]
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[[Category: Nuclear protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:20:14 2008''
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Current revision

Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats

PDB ID 1w9c

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