3c9c
From Proteopedia
Structural Basis of Histone H4 Recognition by p55
Overview
p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a beta-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.
About this Structure
3C9C is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Structural basis of histone H4 recognition by p55., Song JJ, Garlick JD, Kingston RE, Genes Dev. 2008 Apr 28;. PMID:18443147 Page seeded by OCA on Wed May 14 11:32:12 2008
Categories: Drosophila melanogaster | Protein complex | Garlick, J D. | Kingston, R E. | Song, J J. | Chromatin | Chromatin regulator | Chromosomal protein | Dna-binding | Epigenetic | Histone | Nuclear protein | Nucleosome core | Nucleus | P55 | Phosphoprotein | Repressor | Transcription | Transcription regulation | Transcription repressor | Wd repeat | Wd4
