title: Structural genomics of histone tail recognition.
abstract: CONCLUSIONS
  The structural genomics of histone tail recognition web server is an open access resource that presents within mini articles all publicly available experimental structures of histone tails in complex with human proteins. Each article is composed of interactive 3D slides that dissect the structural mechanism underlying the recognition of specific sequences and histone marks. A concise text html-linked to interactive graphics guides the reader through the main features of the interaction. This resource can be used to analyze and compare binding modes across multiple histone recognition modules, to evaluate the chemical tractability of binding sites involved in epigenetic signaling and design small molecule inhibitors.
  
  
  BACKGROUND
  http://www.thesgc.org/resources/histone_tails/
  
  
  BACKGROUND
  matthieu.schapira@utoronto.ca
  
  
  BACKGROUND
  Supplementary data are available at Bioinformatics online.
authors.affiliation: Structural Genomics Consortium, University of Oxford, Headington, Oxford OX37DQ, UK.
authors.forename: Minghua
authors.initials: M
authors.lastname: Wang
authors.forename: Man Wai
authors.initials: MW
authors.lastname: Mok
authors.forename: Hong
authors.initials: H
authors.lastname: Harper
authors.forename: Wen Hwa
authors.initials: WH
authors.lastname: Lee
authors.forename: Jinrong
authors.initials: J
authors.lastname: Min
authors.forename: Stefan
authors.initials: S
authors.lastname: Knapp
authors.forename: Udo
authors.initials: U
authors.lastname: Oppermann
authors.forename: Brian
authors.initials: B
authors.lastname: Marsden
authors.forename: Matthieu
authors.initials: M
authors.lastname: Schapira
mesh_terms: D001665:Binding Sites; D030562:Databases, Protein; D023281:Genomics / Q000379:methods*; D006657:Histones / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D006657:Histones