ArticleThe EMBO journal2004
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
50 citing papers in PubMed, 101 citations in OpenAlex.
- GSK3β-driven phosphorylation of ABLIM1 regulates its interactions with titin cardiac muscle.The Journal of general physiology · 2025Article
- LDB1 establishes multi-enhancer networks to regulate gene expression.Molecular cell · 2025Article
- Utilizing anomalous signals for element identification in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- LDB1 establishes multi-enhancer networks to regulate gene expression.bioRxiv : the preprint server for biology · 2024Article
- Tandem LIM domain-containing proteins, LIMK1 and LMO1, directly bind to force-bearing keratin intermediate filaments.Cell reports · 2024Article
- The PDLIM family of actin-associated proteins and their emerging role in membrane trafficking.Biochemical Society transactions · 2023Review
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Jacob-induced transcriptional inactivation of CREB promotes Aβ-induced synapse loss in Alzheimer's disease.The EMBO journal · 2023Article
- How "Neuronal" Are Human Skin Mast Cells?International journal of molecular sciences · 2022Review
- Bioinformatic Analysis of Structure and Function of LIM Domains of Human Zyxin Family Proteins.International journal of molecular sciences · 2021Article
- Small molecule inhibits T-cell acute lymphoblastic leukaemia oncogenic interaction through conformational modulation of LMO2.Oncotarget · 2020Article
- Crystal structure of human LDB1 in complex with SSBP2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Yeats4 drives ILC lineage commitment via activation ofThe Journal of experimental medicine · 2019Article
- Deciphering RNA-Recognition Patterns of Intrinsically Disordered Proteins.International journal of molecular sciences · 2018Article
- Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegans.Scientific reports · 2017Article
- Fusion-protein-assisted protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2015Article
- In silico design of a DNA-based HIV-1 multi-epitope vaccine for Chinese populations.Human vaccines & immunotherapeutics · 2015Article
- The co-factor of LIM domains (CLIM/LDB/NLI) maintains basal mammary epithelial stem cells and promotes breast tumorigenesis.PLoS genetics · 2014Article
- LIM-domain-only proteins: multifunctional nuclear transcription coregulators that interacts with diverse proteins.Molecular biology reports · 2014Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 complex with Ldb1-LID, providing the first example of a tandem LIM:Ldb1-LID complex and the first structure of a type-B LIM domain. The complex possesses a highly modular structure with Ldb1-LID binding in an extended manner across both LIM domains of LMO4. The interface contains extensive hydrophobic and electrostatic interactions and multiple backbone-backbone hydrogen bonds. A mutagenic screen of Ldb1-LID, assessed by yeast two-hybrid and competition ELISA analysis, identified key features at the interface and revealed that the interaction is tolerant to mutation. These combined properties provide a mechanism for the binding of Ldb1 to numerous LMO and LIM-HD proteins. Furthermore, the modular extended interface may form a general mode of binding to tandem LIM domains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.