3c99: Difference between revisions

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'''Structural Basis of Histone H4 Recognition by p55'''
===Structural Basis of Histone H4 Recognition by p55===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Wd repeat]]
[[Category: Wd repeat]]
[[Category: Wd40]]
[[Category: Wd40]]
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Revision as of 23:03, 28 July 2008

File:3c99.png

Template:STRUCTURE 3c99

Structural Basis of Histone H4 Recognition by p55Structural Basis of Histone H4 Recognition by p55

Template:ABSTRACT PUBMED 18443147

About this StructureAbout this Structure

3C99 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

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 Mon Jul 28 23:03:46 2008

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