2i32
From Proteopedia
(New page: 200px<br /> <applet load="2i32" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i32, resolution 2.700Å" /> '''Structure of a hum...) |
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| - | [[Image:2i32.gif|left|200px]]<br /> | + | [[Image:2i32.gif|left|200px]]<br /><applet load="2i32" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2i32" size=" | + | |
caption="2i32, resolution 2.700Å" /> | caption="2i32, resolution 2.700Å" /> | ||
'''Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly'''<br /> | '''Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone | + | Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes. |
==About this Structure== | ==About this Structure== | ||
| - | 2I32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2I32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2I32 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: histone deposition]] | [[Category: histone deposition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:32 2008'' |
Revision as of 15:48, 21 February 2008
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Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly
Overview
Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes.
About this Structure
2I32 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly., Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R, Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972
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