Sandbox ggc16
From Proteopedia
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==2PQ8 Structure '''Myst Histone Acetyltransferase'''== | ==2PQ8 Structure '''Myst Histone Acetyltransferase'''== | ||
<StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''> | <StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''> | ||
| - | MYST Histone Acetyltransferases (HAT), diverse family of proteins responsible for a variety of functions in eukaryotes. | + | MYST Histone Acetyltransferases (HAT), a diverse family of proteins responsible for a variety of functions in eukaryotes from yeast to humans. These particular histone acetyltransferases are part of the MYST family because of their structure which includes coenzyme A and <scene name='78/782639/Zinc_ion/1'>Zinc Ion</scene>. |
Part of the Myst Family, this histone modifier adds and removes a variety of chemical moieties to histone residues. Such modifications on a single or on several neighboring nucleosomes combine to produce a specific effect on the local chromatin structure. | Part of the Myst Family, this histone modifier adds and removes a variety of chemical moieties to histone residues. Such modifications on a single or on several neighboring nucleosomes combine to produce a specific effect on the local chromatin structure. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI: 10.1021/acschembio.5b00841</ref> or to the article describing Jmol <ref>PMID:11134336</ref> to the rescue.<ref>PMID:10441070</ref>,<ref>PMID:11057899</ref> | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI: 10.1021/acschembio.5b00841</ref> or to the article describing Jmol <ref>PMID:11134336</ref> to the rescue.<ref>PMID:10441070</ref>,<ref>PMID:11057899</ref> | ||
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<scene name='78/782639/13_unknown_atoms_or_ions/1'>Unknown_atoms_or_ions</scene> | <scene name='78/782639/13_unknown_atoms_or_ions/1'>Unknown_atoms_or_ions</scene> | ||
| - | <scene name='78/782639/Zinc_ion/1'> | + | <scene name='78/782639/Zinc_ion/1'>Zinc Ion</scene> |
<scene name='78/782639/Unknown_atoms/1'>Unknown_atoms</scene> | <scene name='78/782639/Unknown_atoms/1'>Unknown_atoms</scene> | ||
Revision as of 13:25, 20 November 2019
2PQ8 Structure Myst Histone Acetyltransferase
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References
- ↑ McCullough CE, Marmorstein R. Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation. ACS Chem Biol. 2016 Mar 18;11(3):632-42. doi: 10.1021/acschembio.5b00841. Epub, 2015 Dec 2. PMID:26555232 doi:http://dx.doi.org/10.1021/acschembio.5b00841
- ↑ Chen CJ, Deng Z, Kim AY, Blobel GA, Lieberman PM. Stimulation of CREB binding protein nucleosomal histone acetyltransferase activity by a class of transcriptional activators. Mol Cell Biol. 2001 Jan;21(2):476-87. doi: 10.1128/MCB.21.2.476-487.2001. PMID:11134336 doi:http://dx.doi.org/10.1128/MCB.21.2.476-487.2001
- ↑ Grant PA, Berger SL. Histone acetyltransferase complexes. Semin Cell Dev Biol. 1999 Apr;10(2):169-77. doi: 10.1006/scdb.1999.0298. PMID:10441070 doi:http://dx.doi.org/10.1006/scdb.1999.0298
- ↑ Cheung P, Allis CD, Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell. 2000 Oct 13;103(2):263-71. doi: 10.1016/s0092-8674(00)00118-5. PMID:11057899 doi:http://dx.doi.org/10.1016/s0092-8674(00)00118-5
