1srk

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[[Image:1srk.gif|left|200px]]
[[Image:1srk.gif|left|200px]]
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{{Structure
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|PDB= 1srk |SIZE=350|CAPTION= <scene name='initialview01'>1srk</scene>
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The line below this paragraph, containing "STRUCTURE_1srk", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY=
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|GENE= ZFPM1, FOG1, FOG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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{{STRUCTURE_1srk| PDB=1srk | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1srk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srk OCA], [http://www.ebi.ac.uk/pdbsum/1srk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1srk RCSB]</span>
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'''Solution structure of the third zinc finger domain of FOG-1'''
'''Solution structure of the third zinc finger domain of FOG-1'''
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[[Category: Matthews, J M.]]
[[Category: Matthews, J M.]]
[[Category: Simpson, R J.Y.]]
[[Category: Simpson, R J.Y.]]
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[[Category: classical zinc finger]]
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[[Category: Classical zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:03:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:03 2008''
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Revision as of 06:03, 3 May 2008

Template:STRUCTURE 1srk

Solution structure of the third zinc finger domain of FOG-1


Overview

Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by an alpha-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an alpha-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the alpha-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the alpha-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.

About this Structure

1SRK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

A classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3., Simpson RJ, Yi Lee SH, Bartle N, Sum EY, Visvader JE, Matthews JM, Mackay JP, Crossley M, J Biol Chem. 2004 Sep 17;279(38):39789-97. Epub 2004 Jul 2. PMID:15234987 Page seeded by OCA on Sat May 3 09:03:49 2008

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