ArticlePloS one2012
Crystal structures of the network-forming short-arm tips of the laminin β1 and γ1 chains.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Beyond MIDAS: AnACS omega · 2026Article
- Article
- Cryo-EM reveals molecular mechanisms underlying the inhibitory effect of netrin-4 on laminin matrix formation.Nature communications · 2025Article
- Identifying the molecular basis of Laminin N-terminal domain CaBiophysical journal · 2024Article
- Observing Dynamic Conformational Changes within the Coiled-Coil Domain of Different Laminin Isoforms Using High-Speed Atomic Force Microscopy.International journal of molecular sciences · 2024Article
- Artificial intelligence and the analysis of cryo-EM data provide structural insight into the molecular mechanisms underlying LN-lamininopathies.Scientific reports · 2023Article
- Laminin N-terminus α31 expression during development is lethal and causes widespread tissue-specific defects in a transgenic mouse model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Organization of the laminin polymer node.Matrix biology : journal of the International Society for Matrix Biology · 2021Article
- Laminin Polymerization and Inherited Disease: Lessons From Genetics.Frontiers in genetics · 2021Review
- Fully synthetic matrices for in vitro culture of primary human intestinal enteroids and endometrial organoids.Biomaterials · 2020Article
- Comprehensive Endogenous Tagging of Basement Membrane Components Reveals Dynamic Movement within the Matrix Scaffolding.Developmental cell · 2020Article
- A deletion in the N-terminal polymerizing domain of laminin β2 is a new mouse model of chronic nephrotic syndrome.Kidney international · 2020Article
- Production of Extracellular Matrix Proteins in the Cytoplasm ofInternational journal of molecular sciences · 2020Article
- Structural biology of laminins.Essays in biochemistry · 2019Review
- Identification and quantification of sites of nitration and oxidation in the key matrix protein laminin and the structural consequences of these modifications.Redox biology · 2019Article
- Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase.Redox biology · 2019Article
- Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Developing defined substrates for stem cell culture and differentiation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Chimeric protein identification of dystrophic, Pierson and other laminin polymerization residues.Matrix biology : journal of the International Society for Matrix Biology · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
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3 authors.
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Abstract
The heterotrimeric laminins are a defining component of basement membranes and essential for tissue formation and function in all animals. The three short arms of the cross-shaped laminin molecule are composed of one chain each and their tips mediate the formation of a polymeric network. The structural basis for laminin polymerisation is unknown. We have determined crystal structures of the short-arm tips of the mouse laminin β1 and γ1 chains, which are grossly similar to the previously determined structure of the corresponding α5 chain region. The short-arm tips consist of a laminin N-terminal (LN) domain that is attached like the head of a flower to a rod-like stem formed by tandem laminin-type epidermal growth factor-like (LE) domains. The LN domain is a β-sandwich with elaborate loop regions that differ between chains. The γ1 LN domain uniquely contains a calcium binding site. The LE domains have little regular structure and are stabilised by cysteines that are disulphide-linked 1-3, 2-4, 5-6 and 7-8 in all chains. The LN surface is not conserved across the α, β and γ chains, but within each chain subfamily there is a striking concentration of conserved residues on one face of the β-sandwich, while the opposite face invariably is shielded by glycans. We propose that the extensive conserved patches on the β and γ LN domains mediate the binding of these two chains to each other, and that the α chain LN domain subsequently binds to the composite β-γ surface. Mutations in the laminin β2 LN domain causing Pierson syndrome are likely to impair the folding of the β2 chain or its ability to form network interactions.
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