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==Solution structure of the C-terminal domain of the HMGB2== | ==Solution structure of the C-terminal domain of the HMGB2== | ||
<StructureSection load='1j3c' size='340' side='right'caption='[[1j3c | <StructureSection load='1j3c' size='340' side='right'caption='[[1j3c]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J3C FirstGlance]. <br> | ||
</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=1j3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3c OCA], [https://pdbe.org/1j3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3c RCSB], [https://www.ebi.ac.uk/pdbsum/1j3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3c ProSAT]</span></td></tr> | </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'>[https://proteopedia.org/fgij/fg.htm?mol=1j3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3c OCA], [https://pdbe.org/1j3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3c RCSB], [https://www.ebi.ac.uk/pdbsum/1j3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HMGB2_PIG HMGB2_PIG] 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) (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sus scrofa]] | ||
[[Category: Kurita | [[Category: Kurita J]] | ||
[[Category: Shimahara | [[Category: Shimahara H]] | ||
[[Category: Tate | [[Category: Tate S]] | ||
[[Category: Yoshida | [[Category: Yoshida M]] | ||
Latest revision as of 02:41, 28 December 2023
Solution structure of the C-terminal domain of the HMGB2Solution structure of the C-terminal domain of the HMGB2
Structural highlights
FunctionHMGB2_PIG 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) (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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