2LXD

Backbone 1H, 13C, and 15N Chemical Shift Assignments for LMO2(LIM2)-Ldb1(LID)

Replaces:  2L3K

Summary for 2LXD

• Entry DOI: 10.2210/pdb2lxd/pdb
• NMR Information: BMRB: 16779
• Descriptor: Rhombotin-2,LIM domain-binding protein 1, ZINC ION (2 entities in total)
• Functional Keywords: lim, ldb1, transcription
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 1
• Total formula weight: 13936.23

Authors

Dastmalchi, S.,Wilkinson-White, L.,Kwan, A.H.,Gamsjaeger, R.,Mackay, J.P.,Matthews, J.M. (deposition date: 2012-08-20, release date: 2012-09-12, Last modification date: 2024-05-15)

Primary citation

Dastmalchi, S.,Wilkinson-White, L.,Kwan, A.H.,Gamsjaeger, R.,Mackay, J.P.,Matthews, J.M.
Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex.
Protein Sci., 21:1768-1774, 2012

PubMed 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.

PubMed: 22936624
DOI: 10.1002/pro.2153

Experimental method

SOLUTION NMR