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1GNF

SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES

Summary for 1GNF
Entry DOI10.2210/pdb1gnf/pdb
DescriptorTRANSCRIPTION FACTOR GATA-1, ZINC ION (2 entities in total)
Functional Keywordszinc finger, transcription regulation
Biological sourceMus musculus (house mouse)
Cellular locationNucleus : P17679
Total number of polymer chains1
Total formula weight5265.35
Authors
Kowalski, K.,Czolij, R.,King, G.F.,Crossley, M.,Mackay, J.P. (deposition date: 1998-10-12, release date: 1999-06-08, Last modification date: 2024-05-01)
Primary citationKowalski, K.,Czolij, R.,King, G.F.,Crossley, M.,Mackay, J.P.
The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG.
J.Biomol.NMR, 13:249-262, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10212985
DOI: 10.1023/A:1008309602929
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-25公开中

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