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Sandbox ggc16

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<StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' scene=''>
<StructureSection load='2pq8' size='340' side='right' caption='Myst Histone Acetyltransferase' 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.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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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:21638687</ref> to the rescue.
== Function ==
== Function ==

Revision as of 09:52, 20 November 2019

2PQ8 Structure Myst Histone Acetyltransferase

Myst Histone Acetyltransferase

Drag the structure with the mouse to rotate

References

  1. 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
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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