2v0f
From Proteopedia
(New page: 200px<br /> <applet load="2v0f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v0f" /> '''BRK DOMAIN FROM HUMAN CHD7'''<br /> ==Over...) |
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'''BRK DOMAIN FROM HUMAN CHD7'''<br /> | '''BRK DOMAIN FROM HUMAN CHD7'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | ||
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- | ==Disease== | ||
- | Known diseases associated with this structure: CHARGE syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608892 608892]], Scoliosis, idiopathic 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608892 608892]] | ||
==About this Structure== | ==About this Structure== | ||
- | 2V0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2V0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:58:32 2008'' |
Revision as of 11:58, 23 January 2008
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BRK DOMAIN FROM HUMAN CHD7
Overview
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.
About this Structure
2V0F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution Structure of the BRK Domains from CHD7., Allen MD, Religa TL, Freund SM, Bycroft M, J Mol Biol. 2007 Jun 9;. PMID:17603073
Page seeded by OCA on Wed Jan 23 13:58:32 2008
Categories: Homo sapiens | Single protein | 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