2v0e: Difference between revisions
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< | ==BRK domain from human CHD7== | ||
<StructureSection load='2v0e' size='340' side='right'caption='[[2v0e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v0e]] 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=2V0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0E FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ckc|2ckc]], [[2v0f|2v0f]]</div></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=2v0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0e OCA], [https://pdbe.org/2v0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0e RCSB], [https://www.ebi.ac.uk/pdbsum/2v0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0e ProSAT]</span></td></tr> | ||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v0e_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v0e ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CHD7 is a member of the chromodomain helicase DNA binding domain (CHD) family of ATP-dependent chromatin remodelling enzymes. It is mutated in CHARGE syndrome, a multiple congenital anomaly condition. CHD7 is one of a subset of CHD proteins, unique to metazoans that contain the BRK domain, a protein module also found in the Brahma/BRG1 family of helicases. We describe here the NMR solution structure of the two BRK domains of CHD7. Each domain has a compact betabetaalphabeta fold. The second domain has a C-terminal extension consisting of two additional helices. The structure differs from those of other domains present in chromatin-associated proteins. | |||
Solution structure of the BRK domains from CHD7.,Allen MD, Religa TL, Freund SM, Bycroft M J Mol Biol. 2007 Aug 31;371(5):1135-40. Epub 2007 Jun 9. PMID:17603073<ref>PMID:17603073</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2v0e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chromodomain-helicase-DNA-binding protein 3D structures|Chromodomain-helicase-DNA-binding protein 3D structures]] | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
== | [[Category: Allen, M D]] | ||
< | [[Category: Bycroft, M]] | ||
[[Category: | [[Category: Freund, S M.V]] | ||
[[Category: Allen, M D | [[Category: Religa, T L]] | ||
[[Category: Bycroft, M | |||
[[Category: Freund, S M.V | |||
[[Category: Religa, T L | |||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Brk domain]] | [[Category: Brk domain]] | ||
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[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||