2msy: Difference between revisions

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==Solution structure of Hox homeodomain==
==Solution structure of Hox homeodomain==
<StructureSection load='2msy' size='340' side='right'caption='[[2msy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2msy' size='340' side='right'caption='[[2msy]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2msy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSY FirstGlance]. <br>
<table><tr><td colspan='2'>[[2msy]] 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=2MSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HOXC9, HOX3B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</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=2msy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msy OCA], [https://pdbe.org/2msy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msy RCSB], [https://www.ebi.ac.uk/pdbsum/2msy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msy 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=2msy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msy OCA], [https://pdbe.org/2msy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msy RCSB], [https://www.ebi.ac.uk/pdbsum/2msy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HXC9_HUMAN HXC9_HUMAN]] Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.  
[https://www.uniprot.org/uniprot/HXC9_HUMAN HXC9_HUMAN] Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
<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: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Han, J]]
[[Category: Han J]]
[[Category: Kim, H]]
[[Category: Kim H]]
[[Category: Lee, B]]
[[Category: Lee B]]
[[Category: Park, S]]
[[Category: Park S]]
[[Category: Homeodomain]]
[[Category: Transcription]]
[[Category: Transcription factor]]

Revision as of 11:06, 8 March 2023

Solution structure of Hox homeodomainSolution structure of Hox homeodomain

Structural highlights

2msy is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HXC9_HUMAN Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.

Publication Abstract from PubMed

The Hox DNA binding domain, the homeodomain, plays critical roles in genetic control of development and cell fate determination. The variable regulatory functions of Hox proteins are accomplished by binding to target DNA sequences and collaborating protein partners that includes human high mobility group B1 (HMGB1). To better understand the interaction between Hox and HMGB1 and the facilitation of Hox-DNA binding by HMGB1, we solved the solution structure of the homeodomain of Hox including the N-terminal arm region (Hoxc9DBD hereafter). In addition, the details of the interaction between these two proteins, as well as DNA binding of the Hox-HMGB1 complex, were investigated by NMR, ITC, and EMSA. The results suggest that binding of the HMGB1 A-box to Hoxc9DBD makes the loop-1 (loop preceding helix-2 of Hoxc9DBD) more access to DNA backbone, which facilitate Hox-DNA binding with enhanced affinity.

Structural insight into the interaction between the Hox and HMGB1 and understanding of the HMGB1-enhancing effect of Hox-DNA binding.,Kim HH, Park SJ, Han JH, Pathak C, Cheong HK, Lee BJ Biochim Biophys Acta. 2015 May;1854(5):449-59. doi: 10.1016/j.bbapap.2015.02.009., Epub 2015 Feb 20. PMID:25707357[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kim HH, Park SJ, Han JH, Pathak C, Cheong HK, Lee BJ. Structural insight into the interaction between the Hox and HMGB1 and understanding of the HMGB1-enhancing effect of Hox-DNA binding. Biochim Biophys Acta. 2015 May;1854(5):449-59. doi: 10.1016/j.bbapap.2015.02.009., Epub 2015 Feb 20. PMID:25707357 doi:http://dx.doi.org/10.1016/j.bbapap.2015.02.009
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