Evidence map›Paper›PMID 10212985›Full record

ArticleJournal of biomolecular NMR1999

The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG.

K Kowalski, R Czolij, G F King, M Crossley, J P Mackay

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Article in Journal of biomolecular NMR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

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  9. Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction.Proceedings of the National Academy of Sciences of the United States of America · 2005
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  10. Article
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  12. Context-dependent regulation of GATA-1 by friend of GATA-1.Proceedings of the National Academy of Sciences of the United States of America · 2004
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

K KowalskiDepartment of Biochemistry, University of Sydney, NSW, Australia.
R Czolij
G F King
M Crossley
J P Mackay

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCarrier ProteinsComputer SimulationDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsGATA1 Transcription FactorMiceModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentCarrier ProteinsDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsGata1 protein, mouseGATA1 Transcription FactorNuclear ProteinsRecombinant ProteinsTranscription FactorsZfpm1 protein, mouse

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.