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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2001-8-27
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pubmed:abstractText |
The nuclear LIM-only (LMO) transcription factors LMO2 and LMO4 play important roles in both normal and leukemic T-cell development. LIM domains are cysteine/histidine-rich domains that contain two structural zinc ions and that function as protein-protein adaptors; members of the LMO family each contain two closely spaced LIM domains. These LMO proteins all bind with high affinity to the nuclear protein LIM domain binding protein 1 (ldb1). The LMO-ldb1 interaction is mediated through the N-terminal LIM domain (LIM1) of LMO proteins and a 38-residue region towards the C-terminus of ldb1 [ldb1(LID)]. Unfortunately, recombinant forms of LMO2 and LMO4 have limited solubility and stability, effectively preventing structural analysis. Therefore, we have designed and constructed a fusion protein in which ldb1(LID) and LIM1 of LMO2 can form an intramolecular complex. The engineered protein, FLIN2 (fusion of the LIM interacting domain of ldb1 and the N-terminal LIM domain of LMO2) has been expressed and purified in milligram quantities. FLIN2 is monomeric, contains significant levels of secondary structure and yields a sharp and well-dispersed one-dimensional (1)H NMR spectrum. The analogous LMO4 protein, FLIN4, has almost identical properties. These data suggest that we will be able to obtain high-resolution structural information about the LMO-ldb1 interactions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LDB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/LIM Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ldb1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lmo2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lmo4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0269-2139
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
493-9
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11522923-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11522923-Amino Acid Sequence,
pubmed-meshheading:11522923-Animals,
pubmed-meshheading:11522923-Binding Sites,
pubmed-meshheading:11522923-Cloning, Molecular,
pubmed-meshheading:11522923-DNA-Binding Proteins,
pubmed-meshheading:11522923-Escherichia coli,
pubmed-meshheading:11522923-Homeodomain Proteins,
pubmed-meshheading:11522923-LIM Domain Proteins,
pubmed-meshheading:11522923-Magnetic Resonance Spectroscopy,
pubmed-meshheading:11522923-Metalloproteins,
pubmed-meshheading:11522923-Mice,
pubmed-meshheading:11522923-Nuclear Proteins,
pubmed-meshheading:11522923-Protein Binding,
pubmed-meshheading:11522923-Protein Engineering,
pubmed-meshheading:11522923-Protein Folding,
pubmed-meshheading:11522923-Protein Structure, Secondary,
pubmed-meshheading:11522923-Recombinant Fusion Proteins,
pubmed-meshheading:11522923-Transcription Factors,
pubmed-meshheading:11522923-Zinc
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pubmed:year |
2001
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pubmed:articleTitle |
Design, production and characterization of FLIN2 and FLIN4: the engineering of intramolecular ldb1:LMO complexes.
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pubmed:affiliation |
Department of Biochemistry, University of Sydney, Sydney, NSW 2006, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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