5e6q: Difference between revisions
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<StructureSection load='5e6q' size='340' side='right'caption='[[5e6q]], [[Resolution|resolution]] 2.31Å' scene=''> | <StructureSection load='5e6q' size='340' side='right'caption='[[5e6q]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e6q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6Q OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5e6q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E6Q FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.305Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5e6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6q OCA], [https://pdbe.org/5e6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e6q RCSB], [https://www.ebi.ac.uk/pdbsum/5e6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6q ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/XRCC1_HUMAN XRCC1_HUMAN] Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gabel | [[Category: Mus musculus]] | ||
[[Category: Gassman | [[Category: Gabel SA]] | ||
[[Category: Kirby | [[Category: Gassman NR]] | ||
[[Category: London | [[Category: Kirby TW]] | ||
[[Category: Pedersen | [[Category: London RE]] | ||
[[Category: Smith | [[Category: Pedersen LC]] | ||
[[Category: Sobhany | [[Category: Smith CE]] | ||
[[Category: Wilson | [[Category: Sobhany M]] | ||
[[Category: Wilson SH]] | |||
Latest revision as of 09:14, 5 July 2023
Importin alpha binding to XRCC1 NLS peptideImportin alpha binding to XRCC1 NLS peptide
Structural highlights
FunctionXRCC1_HUMAN Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Publication Abstract from PubMedWe have characterized the nuclear localization signal (NLS) of XRCC1 structurally using X-ray crystallography and functionally using fluorescence imaging. Crystallography and binding studies confirm the bipartite nature of the XRCC1 NLS interaction with Importin alpha (Impalpha) in which the major and minor binding motifs are separated by >20 residues, and resolve previous inconsistent determinations. Binding studies of peptides corresponding to the bipartite NLS, as well as its major and minor binding motifs, to both wild-type and mutated forms of Impalpha reveal pronounced cooperative binding behavior that is generated by the proximity effect of the tethered major and minor motifs of the NLS. The cooperativity stems from the increased local concentration of the second motif near its cognate binding site that is a consequence of the stepwise binding behavior of the bipartite NLS. We predict that the stepwise dissociation of the NLS from Impalpha facilitates unloading by providing a partially complexed intermediate that is available for competitive binding by Nup50 or the Importin beta binding domain. This behavior provides a basis for meeting the intrinsically conflicting high affinity and high flux requirements of an efficient nuclear transport system. Nuclear Localization of the DNA Repair Scaffold XRCC1: Uncovering the Functional Role of a Bipartite NLS.,Kirby TW, Gassman NR, Smith CE, Pedersen LC, Gabel SA, Sobhany M, Wilson SH, London RE Sci Rep. 2015 Aug 25;5:13405. doi: 10.1038/srep13405. PMID:26304019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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