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Solution structure of a tethered Lmo2 LIM2 /Ldb1 LID complex
Author(s) -
Dastmalchi Siavoush,
WilkinsonWhite Lorna,
Kwan Ann H.,
Gamsjaeger Roland,
Mackay Joel P.,
Matthews Jacqueline M.
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2153
Subject(s) - lim domain , chemistry , microbiology and biotechnology , signal transducing adaptor protein , plasma protein binding , protein–protein interaction , transcription factor , biology , signal transduction , zinc finger , biochemistry , gene
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.