1srk
From Proteopedia
(New page: 200px<br /><applet load="1srk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1srk" /> '''Solution structure of the third zinc finger ...) |
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'''Solution structure of the third zinc finger domain of FOG-1'''<br /> | '''Solution structure of the third zinc finger domain of FOG-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by | + | 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== | ==About this Structure== | ||
| - | 1SRK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1SRK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bartle, N.]] | [[Category: Bartle, N.]] | ||
[[Category: Crossley, M.]] | [[Category: Crossley, M.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S H.Y.]] |
| - | [[Category: Mackay, J | + | [[Category: Mackay, J P.]] |
| - | [[Category: Matthews, J | + | [[Category: Matthews, J M.]] |
| - | [[Category: Simpson, R | + | [[Category: Simpson, R J.Y.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: classical zinc finger]] | [[Category: classical zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:30 2008'' |
Revision as of 13:04, 21 February 2008
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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 with as ligand. 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
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