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
A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions [link]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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