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Article

Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.

The EMBO journal - 15 Sept 2004

Deane Janet E, Ryan Daniel P, Sunde Margaret, Maher Megan J, Guss J Mitchell, Visvader Jane E, Matthews Jacqueline M

Abstract excerpt

Nuclear LIM-only (LMO) and LIM-homeodomain (LIM-HD) proteins have important roles in cell fate determination, organ development and oncogenesis. These proteins contain tandemly arrayed LIM domains that bind the LIM interaction domain (LID) of the nuclear adaptor protein LIM domain-binding protein-1 (Ldb1). We have determined a high-resolution X-ray crystal structure of LMO4, a putative breast oncoprotein, in...

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Share to Adaptor Proteins, Signal Transducing
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 15343268
DOI: 10.1038/sj.emboj.7600376
PMCID: PMC517615

Genes

LMO4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.PMID 15343268Read ↗

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The LIM domain is a modular protein-binding interfaceSemantic proximity Read ↗

Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex.Semantic proximity Read ↗

LIM domains: multiple roles as adapters and functional modifiers in protein interactionsSemantic proximity Read ↗

LMO7 and LIMCH1 interact with LRIG proteins in lung cancer, with prognostic implications for early-stage diseaseSemantic proximity Read ↗

Crystal structure of human LDB1 in complex with SSBP2Semantic proximity Read ↗

The LIM domain gene <i>LMO4</i> inhibits differentiation of mammary epithelial cells <i>in vitro</i> and is overexpressed in breast cancerSemantic proximity Read ↗

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