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

Gadd, MS; Jacques, DA; Nisevic, I; Craig, VJ; Kwan, AH; Guss, JM; Matthews, JM

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

Gadd, MS Jacques, DA

Nisevic, I Craig, VJ Kwan, AH Guss, JM Matthews, JM

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Publication Type:: Journal Article
Citation:: Journal of Biological Chemistry, 2013, 288 (30), pp. 21924 - 21935
Issue Date:: 2013-07-26

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Field	Value	Language
dc.contributor.author	Gadd, MS	en_US
dc.contributor.author	Jacques, DA https://orcid.org/0000-0002-6426-4510	en_US
dc.contributor.author	Nisevic, I	en_US
dc.contributor.author	Craig, VJ	en_US
dc.contributor.author	Kwan, AH	en_US
dc.contributor.author	Guss, JM	en_US
dc.contributor.author	Matthews, JM	en_US
dc.date.issued	2013-07-26	en_US
dc.identifier.citation	Journal of Biological Chemistry, 2013, 288 (30), pp. 21924 - 21935	en_US
dc.identifier.issn	0021-9258	en_US
dc.identifier.uri	http://hdl.handle.net/10453/117207
dc.description.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.	en_US
dc.relation.ispartof	Journal of Biological Chemistry	en_US
dc.relation.isbasedon	10.1074/jbc.M113.478586	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Mice	en_US
dc.subject.mesh	Saccharomyces cerevisiae	en_US
dc.subject.mesh	Transcription Factors	en_US
dc.subject.mesh	Crystallography, X-Ray	en_US
dc.subject.mesh	Two-Hybrid System Techniques	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Structure, Tertiary	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Mutation	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	LIM-Homeodomain Proteins	en_US
dc.title	A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions	en_US
dc.type	Journal Article
utslib.citation.volume	30	en_US
utslib.citation.volume	288	en_US
utslib.for	060108 Protein Trafficking	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	closed_access
pubs.issue	30	en_US
pubs.publication-status	Published	en_US
pubs.volume	288	en_US

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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/117207