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dc.contributor.authorDastmalchi, S
dc.contributor.authorWilkinson-White, L
dc.contributor.authorKwan, AH
dc.contributor.authorGamsjaeger, R
dc.contributor.authorMackay, JP
dc.contributor.authorMatthews, JM
dc.date.accessioned2018-08-26T08:04:24Z
dc.date.available2018-08-26T08:04:24Z
dc.date.issued2012
dc.identifier.urihttp://dspace.tbzmed.ac.ir:8080/xmlui/handle/123456789/49556
dc.description.abstractLIM-only protein 2, Lmo2, is a regulatory protein that is essential for hematopoietic development and inappropriate overexpression of Lmo2 in T-cells contributes to T-cell leukemia. It exerts its functions by mediating protein-protein interactions and nucleating multicomponent transcriptional complexes. Lmo2 interacts with LIM domain binding protein 1 (Ldb1) through the tandem LIM domains of Lmo2 and the LIM interaction domain (LID) of Ldb1. Here, we present the solution structure of the LIM2 domain of Lmo2 bound to Ldb1(LID). The ordered regions of Ldb1 in this complex correspond well with binding hotspots previously defined by mutagenic studies. Comparisons of this Lmo2(LIM2)-Ldb1(LID) structure with previously determined structures of the Lmo2/Ldb1(LID) complexes lead to the conclusion that modular binding of tandem LIM domains in Lmo2 to tandem linear motifs in Ldb1 is accompanied by several disorder-to-order transitions and/or conformational changes in both proteins.
dc.language.isoEnglish
dc.relation.ispartofPROTEIN SCIENCE
dc.subjectLmo2
dc.subjectLdb1
dc.subjectNMR structure
dc.subjectmodular binding
dc.titleSolution structure of a tethered Lmo2(LIM2)/Ldb1(LID) complex
dc.typeArticle
dc.citation.volume21
dc.citation.issue11
dc.citation.spage1768
dc.citation.epage1774
dc.citation.indexWeb of science
dc.identifier.DOIhttps://doi.org/10.1002/pro.2153


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