2iij
From Proteopedia
(New page: 200px<br /><applet load="2iij" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iij" /> '''Structure of human Asf1a in complex with his...) |
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| - | [[Image:2iij.jpg|left|200px]]<br /><applet load="2iij" size=" | + | [[Image:2iij.jpg|left|200px]]<br /><applet load="2iij" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2iij" /> | caption="2iij" /> | ||
'''Structure of human Asf1a in complex with histone H3'''<br /> | '''Structure of human Asf1a in complex with histone H3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Asf1 is a histone chaperone that favors histone H3/H4 assembly and | + | 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== | ==About this Structure== | ||
| - | 2IIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2IIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIJ OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the histone chaperone | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292837 17292837] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Agez, M.]] | [[Category: Agez, M.]] | ||
[[Category: Guerois, R.]] | [[Category: Guerois, R.]] | ||
| - | [[Category: Heijenoort, C | + | [[Category: Heijenoort, C van.]] |
[[Category: Mann, C.]] | [[Category: Mann, C.]] | ||
[[Category: Ochsenbein, F.]] | [[Category: Ochsenbein, F.]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:15 2008'' |
Revision as of 15:53, 21 February 2008
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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 Thu Feb 21 17:53:15 2008
