2e50

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{{STRUCTURE_2e50| PDB=2e50 | SCENE= }}
{{STRUCTURE_2e50| PDB=2e50 | SCENE= }}
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'''Crystal structure of SET/TAF-1beta/INHAT'''
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===Crystal structure of SET/TAF-1beta/INHAT===
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==Overview==
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Histone chaperones assemble and disassemble nucleosomes in an ATP-independent manner and thus regulate the most fundamental step in the alteration of chromatin structure. The molecular mechanisms underlying histone chaperone activity remain unclear. To gain insights into these mechanisms, we solved the crystal structure of the functional domain of SET/TAF-Ibeta/INHAT at a resolution of 2.3 A. We found that SET/TAF-Ibeta/INHAT formed a dimer that assumed a "headphone"-like structure. Each subunit of the SET/TAF-Ibeta/INHAT dimer consisted of an N terminus, a backbone helix, and an "earmuff" domain. It resembles the structure of the related protein NAP-1. Comparison of the crystal structures of SET/TAF-Ibeta/INHAT and NAP-1 revealed that the two proteins were folded similarly except for an inserted helix. However, their backbone helices were shaped differently, and the relative dispositions of the backbone helix and the earmuff domain between the two proteins differed by approximately 40 degrees . Our biochemical analyses of mutants revealed that the region of SET/TAF-Ibeta/INHAT that is engaged in histone chaperone activity is the bottom surface of the earmuff domain, because this surface bound both core histones and double-stranded DNA. This overlap or closeness of the activity surface and the binding surfaces suggests that the specific association among SET/TAF-Ibeta/INHAT, core histones, and double-stranded DNA is requisite for histone chaperone activity. These findings provide insights into the possible mechanisms by which histone chaperones assemble and disassemble nucleosome structures.
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(as it appears on PubMed at http://www.pubmed.gov), where 17360516 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17360516}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity., Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4285-90. Epub 2007 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17360516 17360516]
Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity., Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4285-90. Epub 2007 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17360516 17360516]
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Purification, crystallization and preliminary X-ray diffraction analysis of human oncoprotein SET/TAF-1beta., Muto S, Senda M, Adachi N, Suzuki T, Nagai R, Senda T, Horikoshi M, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):712-4. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039562 15039562]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Pp2ai]]
[[Category: Pp2ai]]
[[Category: Set]]
[[Category: Set]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:40:13 2008''

Revision as of 08:40, 29 July 2008

Image:2e50.png

Template:STRUCTURE 2e50

Crystal structure of SET/TAF-1beta/INHAT

Template:ABSTRACT PUBMED 17360516

About this Structure

2E50 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity., Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4285-90. Epub 2007 Mar 6. PMID:17360516

Purification, crystallization and preliminary X-ray diffraction analysis of human oncoprotein SET/TAF-1beta., Muto S, Senda M, Adachi N, Suzuki T, Nagai R, Senda T, Horikoshi M, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):712-4. Epub 2004, Mar 23. PMID:15039562

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