| Literature DB >> 27050258 |
Damiaan E H F Mevius1, Yunpeng Shen1, Masayo Morishita1, Eric di Luccio1.
Abstract
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.Entities:
Keywords: Schizosaccharomyces pombe; Set7; X-ray crystallography; histone methyltransferase; histone modifications
Mesh:
Substances:
Year: 2016 PMID: 27050258 PMCID: PMC4822981 DOI: 10.1107/S2053230X16003794
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056