5uwp: Difference between revisions

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 ==Crystal Structure of mDia2 NES Peptide in complex with CRM1-Ran-RanBP1==
-<StructureSection load='5uwp' size='340' side='right' caption='[[5uwp]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+<StructureSection load='5uwp' size='340' side='right'caption='[[5uwp]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5uwp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UWP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5uwp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UWP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.054&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uwi|5uwi]], [[5uwh|5uwh]], [[5uwj|5uwj]], [[5uwu|5uwu]], [[5uwo|5uwo]], [[5uwq|5uwq]], [[5uwr|5uwr]], [[5uws|5uws]], [[5uwt|5uwt]], [[5uww|5uww]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<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=5uwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwp OCA], [http://pdbe.org/5uwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uwp RCSB], [http://www.ebi.ac.uk/pdbsum/5uwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwp 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=5uwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uwp OCA], [https://pdbe.org/5uwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uwp RCSB], [https://www.ebi.ac.uk/pdbsum/5uwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uwp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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_YEAST XPO1_YEAST]] Receptor for the leucine-rich nuclear export signal (NES). [[http://www.uniprot.org/uniprot/YRB1_YEAST YRB1_YEAST]] Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1 and GSP2.
+[https://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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Nuclear export receptor CRM1 binds highly variable nuclear export signals (NESs) in hundreds of different cargoes. Previously we have shown that CRM1 binds NESs in both polypeptide orientations (Fung et al., 2015). Here, we show crystal structures of CRM1 bound to eight additional NESs which reveal diverse conformations that range from loop-like to all-helix, which occupy different extents of the invariant NES-binding groove. Analysis of all NES structures show 5-6 distinct backbone conformations where the only conserved secondary structural element is one turn of helix that binds the central portion of the CRM1 groove. All NESs also participate in main chain hydrogen bonding with human CRM1 Lys568 side chain, which acts as a specificity filter that prevents binding of non-NES peptides. The large conformational range of NES backbones explains the lack of a fixed pattern for its 3-5 hydrophobic anchor residues, which in turn explains the large array of peptide sequences that can function as NESs.
-Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals.,Fung HY, Fu SC, Chook YM Elife. 2017 Mar 10;6. pii: e23961. doi: 10.7554/eLife.23961. PMID:28282025<ref>PMID:28282025</ref>
+==See Also==
+*[[Exportin 3D structures|Exportin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
-</div>
-<div class="pdbe-citations 5uwp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Chook, Y M]]
+[[Category: Homo sapiens]]
-[[Category: Fung, H Y.J]]
+[[Category: Large Structures]]
-[[Category: Heat repeat]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Karyopherin]]
+[[Category: Chook YM]]
-[[Category: Ne]]
+[[Category: Fung HYJ]]
-[[Category: Nuclear export]]
-[[Category: Protein transport]]