1ofc: Difference between revisions

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[[Image:1ofc.gif|left|200px]]
{{Seed}}
[[Image:1ofc.png|left|200px]]


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{{STRUCTURE_1ofc|  PDB=1ofc  |  SCENE=  }}  
{{STRUCTURE_1ofc|  PDB=1ofc  |  SCENE=  }}  


'''NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE'''
===NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE===




==Overview==
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Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
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{{ABSTRACT_PUBMED_14536084}}


==About this Structure==
==About this Structure==
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[[Category: Nucleosome recognition]]
[[Category: Nucleosome recognition]]
[[Category: Sant domain]]
[[Category: Sant domain]]
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Revision as of 01:57, 29 July 2008

File:1ofc.png

Template:STRUCTURE 1ofc

NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE

Template:ABSTRACT PUBMED 14536084

About this Structure

1OFC is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI., Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW, Mol Cell. 2003 Aug;12(2):449-60. PMID:14536084

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