ArticleThe EMBO journal2000
Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 189 citations in OpenAlex.
- 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
- Chain-specificity of laminin α1-5 LG45 modules in the recognition of carbohydrate-linked receptors and intramolecular binding.Scientific reports · 2023Article
- Collagen a1(XI) structure prediction by Alphafold 2.Proceedings. International Conference on Computational Science and Computational Intelligence · 2022Article
- What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022Review
- Plasticity of the lettuce infectious yellows virus minor coat protein (CPm) in mediating the foregut retention and transmission of a chimeric CPm mutant by whitefly vectors.The Journal of general virology · 2021Article
- Basement Membrane Extracellular Matrix Proteins in Pulmonary Vascular and Right Ventricular Remodeling in Pulmonary Hypertension.American journal of respiratory cell and molecular biology · 2021Article
- Zebrafish as a Model to Evaluate a CRISPR/Cas9-Based Exon Excision Approach as a Future Treatment Option forInternational journal of molecular sciences · 2021Article
- Proteins Binding to the Carbohydrate HNK-1: Common Origins?International journal of molecular sciences · 2021Article
- EYS mutations and implementation of minigene assay for variant classification in EYS-associated retinitis pigmentosa in northern Sweden.Scientific reports · 2021Article
- HNK-1 sulfotransferase modulates α-dystroglycan glycosylation by 3-O-sulfation of glucuronic acid on matriglycan.Glycobiology · 2020Article
- Article
- biAb Mediated Restoration of the Linkage between Dystroglycan and Laminin-211 as a Therapeutic Approach for α-Dystroglycanopathies.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- Inhibitor discovery for the E. coli meningitis virulence factor IbeA from homology modeling and virtual screening.Journal of computer-aided molecular design · 2020Article
- The Non-Fibrillar Side of Fibrosis: Contribution of the Basement Membrane, Proteoglycans, and Glycoproteins to Myocardial Fibrosis.Journal of cardiovascular development and disease · 2019Review
- Structural biology of laminins.Essays in biochemistry · 2019Review
- Cell Biology of Intracellular Adaptation ofMicrobiology spectrum · 2019Review
- Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019Review
- Current understanding and treatment of cardiac and skeletal muscle pathology in laminin-α2 chain-deficient congenital muscular dystrophy.The application of clinical genetics · 2019Article
- Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.Frontiers in molecular biosciences · 2019Review
- Novel LAMA2 Gene Mutations Associated with Merosin-Deficient Congenital Muscular DystrophyIranian biomedical journal · 2018Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency.
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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.