1nyh

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[[Image:1nyh.jpg|left|200px]]
[[Image:1nyh.jpg|left|200px]]
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{{Structure
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|PDB= 1nyh |SIZE=350|CAPTION= <scene name='initialview01'>1nyh</scene>, resolution 3.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1nyh", creates the "Structure Box" on the page.
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|GENE= SIR4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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{{STRUCTURE_1nyh| PDB=1nyh | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyh OCA], [http://www.ebi.ac.uk/pdbsum/1nyh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nyh RCSB]</span>
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'''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''
'''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''
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[[Category: Moazed, D.]]
[[Category: Moazed, D.]]
[[Category: Tanny, J C.]]
[[Category: Tanny, J C.]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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[[Category: repressor]]
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[[Category: Repressor]]
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[[Category: transcription regulation]]
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[[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 Sun Mar 30 22:37:18 2008''
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Revision as of 00:08, 3 May 2008

Template:STRUCTURE 1nyh

Crystal Structure of the Coiled-coil Dimerization Motif of Sir4


Overview

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.

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 Page seeded by OCA on Sat May 3 03:08:21 2008

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