2iij: Difference between revisions

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[[Image:2iij.jpg|left|200px]]
[[Image:2iij.jpg|left|200px]]


{{Structure
<!--
|PDB= 2iij |SIZE=350|CAPTION= <scene name='initialview01'>2iij</scene>
The line below this paragraph, containing "STRUCTURE_2iij", creates the "Structure Box" on the page.
|SITE=
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|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= ASF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_2iij| PDB=2iij |  SCENE= }}  
|RELATEDENTRY=[[1tey|1tey]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iij OCA], [http://www.ebi.ac.uk/pdbsum/2iij PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iij RCSB]</span>
}}


'''Structure of human Asf1a in complex with histone H3'''
'''Structure of human Asf1a in complex with histone H3'''
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[[Category: Mann, C.]]
[[Category: Mann, C.]]
[[Category: Ochsenbein, F.]]
[[Category: Ochsenbein, F.]]
[[Category: protein-protein complex]]
[[Category: Protein-protein complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:32:51 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:51 2008''

Revision as of 04:32, 4 May 2008

File:2iij.jpg

Template:STRUCTURE 2iij

Structure of human Asf1a in complex with histone H3


Overview

Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.

About this Structure

2IIJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights., Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F, Structure. 2007 Feb;15(2):191-9. PMID:17292837 Page seeded by OCA on Sun May 4 07:32:51 2008

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