3gb8

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<StructureSection load='3gb8' size='340' side='right'caption='[[3gb8]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3gb8' size='340' side='right'caption='[[3gb8]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3gb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GB8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3gb8]] 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=3GB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GB8 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRM1, XPO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNUT1, SNUPN, SPN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gb8 OCA], [https://pdbe.org/3gb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3gb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gb8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gb8 OCA], [https://pdbe.org/3gb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gb8 RCSB], [https://www.ebi.ac.uk/pdbsum/3gb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gb8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> [[https://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>
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3gb8 ConSurf].
</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=3gb8 ConSurf].
<div style="clear:both"></div>
<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 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 A structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain. The LR-NES is a combined alpha-helical-extended structure that occupies a hydrophobic groove between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic pattern, preference for intervening electronegative residues and inhibition by leptomycin B. The second nuclear export signal epitope is a basic surface on the snurportin 1 nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES site. Multipartite recognition of individually weak nuclear export signal epitopes may be common to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity LR-NES. Similar energetic construction is also used in multipartite nuclear localization signals to provide broad substrate specificity and rapid evolution in nuclear transport.
 
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Structural basis for leucine-rich nuclear export signal recognition by CRM1.,Dong X, Biswas A, Suel KE, Jackson LK, Martinez R, Gu H, Chook YM Nature. 2009 Apr 30;458(7242):1136-41. Epub 2009 Apr 1. PMID:19339969<ref>PMID:19339969</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3gb8" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Biswas, A]]
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[[Category: Biswas A]]
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[[Category: Chook, Y M]]
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[[Category: Chook YM]]
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[[Category: Dong, X]]
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[[Category: Dong X]]
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[[Category: Gu, H]]
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[[Category: Gu H]]
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[[Category: Jackson, L K]]
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[[Category: Jackson LK]]
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[[Category: Martinez, R]]
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[[Category: Martinez R]]
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[[Category: Suel, K E]]
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[[Category: Suel KE]]
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[[Category: Host-virus interaction]]
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[[Category: Mrna transport]]
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[[Category: Nuclear transport complex]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Protein transport]]
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[[Category: Rna-binding]]
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[[Category: Transport]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of CRM1/Snurportin-1 complex

PDB ID 3gb8

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