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

Gadd, MS and Jacques, DA and Nisevic, I and Craig, VJ and Kwan, AH and Guss, JM and Matthews, JM (2013) A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions. Journal of Biological Chemistry. pp. 21924-21935.

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

Item Type: Article
Additional Information: pubid: 11 nvp_institute: NIBR contributor_address: (Gadd, Jacques, Nisevic, Craig, Kwan, Guss, Matthews) School of Molecular Bioscience, Building G08, University of Sydney, NSW 2006, Australia (Jacques) Medical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Ave., Cambridge CB2 0QH, United Kingdom (Craig) Novartis Insts. for BioMedical Research, Klybeckstr. 141, 4057 Basel, Switzerland
Date Deposited: 13 Oct 2015 13:13
Last Modified: 13 Oct 2015 13:13
URI: https://oak.novartis.com/id/eprint/21865

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