1gnf
From Proteopedia
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SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES
Overview
Zinc fingers (ZnFs) are generally regarded as DNA-binding motifs. However, a number of recent reports have implicated particular ZnFs in the, mediation of protein-protein interactions. The N-terminal ZnF of GATA-1, (NF) is one such finger, having been shown to interact with a number of, other proteins, including the recently discovered transcriptional, co-factor FOG. Here we solve the three-dimensional structure of the NF in, solution using multidimensional 1H/15N NMR spectroscopy, and we use 1H/15N, spin relaxation measurements to investigate its backbone dynamics. The, structure consists of two distorted beta-hairpins and a single, alpha-helix, and is similar to that of the C-terminal ZnF of chicken, GATA-1. Comparisons of the NF structure with those of other C4-type zinc, binding motifs, including hormone receptor and LIM domains, also reveal, substantial structural homology. Finally, we use the structure to map the, spatial locations of NF residues shown by mutagenesis to be essential for, FOG binding, and demonstrate that these residues all lie on a single face, of the NF. Notably, this face is well removed from the putative, DNA-binding face of the NF, an observation which is suggestive of, simultaneous roles for the NF; that is, stabilisation of GATA-1 DNA, complexes and recruitment of FOG to GATA-1-controlled promoter regions.
About this Structure
1GNF is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG., Kowalski K, Czolij R, King GF, Crossley M, Mackay JP, J Biomol NMR. 1999 Mar;13(3):249-62. PMID:10212985
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