Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 72, Issue -, Pages 263-268Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X16003794
Keywords
histone modifications; histone methyltransferase; Schizosaccharomyces pombe; Set7; X-ray crystallography
Funding
- Astex Pharmaceuticals, Cambridge, England [KNU 2014-04260000, KNU 2014-1440000]
- Basic Science Research Program of the National Research Foundation of Korea (NRF) - Ministry of Education, Science and Technology [NRF-2013R1A1A-2012486]
- Grants-in-Aid for Scientific Research [23000012] Funding Source: KAKEN
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Dysfunction of histone-modifying enzymes affects chromatin regulation and is involved in carcinogenesis, tumour progression and other diseases. Histone methyltransferases are a family of key histone-modifying enzymes, but their structures, functions and mechanisms are incompletely understood, thus constraining drug-design efforts. Here, preliminary steps towards structure-function studies of Schizosaccharomyces pombe Set7, a putative histone methyltransferase and the first yeast full-length SET-domain-containing protein to be studied using X-ray crystallography, are reported. The methods from cloning to X-ray diffraction and phasing are discussed and the results will aid in prospective studies of histone-modifying enzymes.
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