ArticleProtein science : a publication of the Protein Society2012
Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Biochemical Feature of LMO2 Interactome and LMO2 Function Prospect.Medical science monitor basic research · 2020Article
- LMO2 Oncoprotein Stability in T-Cell Leukemia Requires Direct LDB1 Binding.Molecular and cellular biology · 2016Article
- Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex.Scientific reports · 2014Article
- Article
- Structural basis for LMO2-driven recruitment of the SCL:E47bHLH heterodimer to hematopoietic-specific transcriptional targets.Cell reports · 2013Article
- LIM-domain-only proteins in cancer.Nature reviews. Cancer · 2013Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LIM-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.
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