1srk
From Proteopedia
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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 ZN 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
Page seeded by OCA on Wed Nov 21 02:36:22 2007
