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2v0e
From Proteopedia
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| - | [[Image:2v0e.gif|left|200px]] | ||
| - | + | ==BRK domain from human CHD7== | |
| - | + | <StructureSection load='2v0e' size='340' side='right'caption='[[2v0e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == 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. | 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> | |
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| - | + | 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> | |
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| - | + | ==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: Freund, S M.V]] | ||
| + | [[Category: Religa, T L]] | ||
| + | [[Category: Atp-binding]] | ||
| + | [[Category: Brk domain]] | ||
| + | [[Category: Charge syndrome]] | ||
| + | [[Category: Chd7]] | ||
| + | [[Category: Chromatin regulator]] | ||
| + | [[Category: Disease mutation]] | ||
| + | [[Category: Dna-binding]] | ||
| + | [[Category: Helicase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Nuclear protein]] | ||
| + | [[Category: Nucleotide-binding]] | ||
| + | [[Category: Phosphorylation]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Transcription regulation]] | ||
Current revision
BRK domain from human CHD7
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Categories: Human | Large Structures | Allen, M D | Bycroft, M | Freund, S M.V | Religa, T L | Atp-binding | Brk domain | Charge syndrome | Chd7 | Chromatin regulator | Disease mutation | Dna-binding | Helicase | Hydrolase | Nuclear protein | Nucleotide-binding | Phosphorylation | Transcription | Transcription regulation
