1ofc

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{{STRUCTURE_1ofc| PDB=1ofc | SCENE= }}
{{STRUCTURE_1ofc| PDB=1ofc | SCENE= }}
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'''NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE'''
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===NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 14536084 is the PubMed ID number.
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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

Image: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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