1ofc: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Single protein]]

[[Category: Grune, T.]]

[[Category: Muller, C.W.]]

[[Category: Muller, C W.]]

[[Category: G4D]]

[[Category: GLC]]

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[[Category: sant domain]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Grune, T.]]
-[[Category: Muller, C.W.]]
+[[Category: Muller, C W.]]
 [[Category: G4D]]
 [[Category: GLC]]
@@ Line 24: / Line 24: @@
 [[Category: sant domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:57:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:05 2008''