A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions. Gadd, M., Jacques, D., Nisevic, I., Craig, V., Kwan, A., Guss, J., & Matthews, J. Journal of Biological Chemistry, 288(30):21924-21935, 2013. cited By 18
Paper doi abstract bibtex Background: A putative intramolecular interaction in the Islet 1 (Isl1) transcription factor inhibits DNA binding. Results: An intramolecular interaction between the LIM domains and LIM homeobox 3 (Lhx3)-binding domain in Isl1 was characterized. Conclusion: The intramolecular interaction within Isl1 is weak but specific. Significance: This interaction likely prevents unproductive binding in the absence of cofactor proteins. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
@ARTICLE{Gadd201321924,
author={Gadd, M.S. and Jacques, D.A. and Nisevic, I. and Craig, V.J. and Kwan, A.H. and Guss, J.M. and Matthews, J.M.},
title={A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions},
journal={Journal of Biological Chemistry},
year={2013},
volume={288},
number={30},
pages={21924-21935},
doi={10.1074/jbc.M113.478586},
note={cited By 18},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84881241858&doi=10.1074%2fjbc.M113.478586&partnerID=40&md5=cfc9fa9ab03999ad0f1b50be0b2d6883},
affiliation={School of Molecular Bioscience, Building G08, University of Sydney, NSW 2006, Australia; Medical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Ave., Cambridge CB2 0QH, United Kingdom; Novartis Insts. for BioMedical Research, Klybeckstr. 141, 4057 Basel, Switzerland},
abstract={Background: A putative intramolecular interaction in the Islet 1 (Isl1) transcription factor inhibits DNA binding. Results: An intramolecular interaction between the LIM domains and LIM homeobox 3 (Lhx3)-binding domain in Isl1 was characterized. Conclusion: The intramolecular interaction within Isl1 is weak but specific. Significance: This interaction likely prevents unproductive binding in the absence of cofactor proteins. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.},
keywords={Binding domain; Cofactors; DNA binding; Intermolecular interactions; Intramolecular interactions; LIM domain; Structural basis, Biochemistry; Biology, Proteins, binding protein; DNA; LIM domain binding protein 1; LIM homeodomain protein; LIM homeodomain protein Islet 1; transcription factor LHX3; unclassified drug, amino acid composition; amino acid sequence; amino acid substitution; article; binding affinity; controlled study; crystal structure; DNA binding; genetic complementation; inhibition kinetics; molecular cloning; molecular interaction; mouse; nonhuman; nuclear magnetic resonance spectroscopy; nucleotide sequence; priority journal; protein aggregation; protein binding; protein domain; protein expression; protein structure; structural homology; two hybrid system, Competitive Binding; LIM-Homeodomain Transcription Factors; Protein-Nucleic Acid Interaction; Protein-Protein Interactions; Structural Biology; Tissue-specific Transcription Factors; Transcription Regulation, Amino Acid Sequence; Animals; Binding Sites; Crystallography, X-Ray; LIM-Homeodomain Proteins; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae; Transcription Factors; Two-Hybrid System Techniques},
correspondence_address1={Matthews, J.M.; School of Molecular Bioscience, , NSW 2006, Australia; email: jacqui.matthews@sydney.edu.au},
issn={00219258},
coden={JBCHA},
pubmed_id={23750000},
language={English},
abbrev_source_title={J. Biol. Chem.},
document_type={Article},
source={Scopus},
}
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