2yrq: Difference between revisions
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==Solution structure of the tandem HMG box domain from Human High mobility group protein B1== | ==Solution structure of the tandem HMG box domain from Human High mobility group protein B1== | ||
<StructureSection load='2yrq' size='340' side='right' caption='[[2yrq | <StructureSection load='2yrq' size='340' side='right'caption='[[2yrq]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yrq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2yrq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YRQ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yrq OCA], [https://pdbe.org/2yrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yrq RCSB], [https://www.ebi.ac.uk/pdbsum/2yrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yrq ProSAT], [https://www.topsan.org/Proteins/RSGI/2yrq TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Harada T]] | ||
[[Category: | [[Category: Kigawa T]] | ||
[[Category: | [[Category: Koshiba S]] | ||
[[Category: Tomizawa | [[Category: Tomizawa T]] | ||
[[Category: Watanabe | [[Category: Watanabe S]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 22:16, 29 May 2024
Solution structure of the tandem HMG box domain from Human High mobility group protein B1Solution structure of the tandem HMG box domain from Human High mobility group protein B1
Structural highlights
FunctionHMGB1_HUMAN DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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