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1nyh

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{{STRUCTURE_1nyh| PDB=1nyh | SCENE= }}
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'''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''
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===Crystal Structure of the Coiled-coil Dimerization Motif of Sir4===
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==Overview==
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The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin.
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(as it appears on PubMed at http://www.pubmed.gov), where 12791253 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12791253}}
==About this Structure==
==About this Structure==
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[[Category: Repressor]]
[[Category: Repressor]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:08:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:16:33 2008''

Revision as of 23:16, 28 July 2008

Image:1nyh.png

Template:STRUCTURE 1nyh

Crystal Structure of the Coiled-coil Dimerization Motif of Sir4

Template:ABSTRACT PUBMED 12791253

About this Structure

1NYH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3., Chang JF, Hall BE, Tanny JC, Moazed D, Filman D, Ellenberger T, Structure. 2003 Jun;11(6):637-49. PMID:12791253

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