2i32: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2i32, resolution 2.700Å" />

'''Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2I32 OCA].

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==

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[[Category: histone deposition]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:40:~~05 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:32 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="2i32, resolution 2.700&Aring;" />
 '''Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly'''<br />
 ==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.
+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==
-I32 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I32 OCA].
+I32 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==
@@ Line 23: / Line 22: @@
 [[Category: histone deposition]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:40:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:32 2008''