ArticleNature communications2015
Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 92 citations in OpenAlex.
- Discovery of a secretedGut microbes · 2026Article
- Synthesis of Polyhydroxylated Pyrrolidinyl Analogs of Sugar Nucleotides. Experimental and Computational Studies on Their Interactions With GalNAC-T's.Chembiochem : a European journal of chemical biology · 2026Article
- A single catalytic domain residue regulates the substrate specificity of a mucin-type O-glycosyltransferase in salivary gland function.bioRxiv : the preprint server for biology · 2025Article
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Rational Design of Dual-Domain Binding Inhibitors forJACS Au · 2024Article
- A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues.Nature communications · 2024Article
- An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.Science advances · 2024Article
- Abnormal glycosylation in glioma: related changes in biology, biomarkers and targeted therapy.Biomarker research · 2023Review
- Molecular Recognition of GalNAc in Mucin-Type O-Glycosylation.Accounts of chemical research · 2023Review
- The effect of a methyl group on structure and function: Serine vs. threonine glycosylation and phosphorylation.Frontiers in molecular biosciences · 2023Review
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A).Communications biology · 2022Article
- CAR T cells redirected against tumor-specific antigen glycoforms: can low-sugar antigens guarantee a sweet success?Frontiers of medicine · 2022Review
- Structural basis for the synthesis of the core 1 structure by C1GalT1.Nature communications · 2022Article
- Atomic and Specificity Details of Mucin 1JACS Au · 2022Article
- Nanomechanical Study of Enzyme: Coenzyme Complexes: Bipartite Sites in Plastidic Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Article
- Role of GALNT2 on Insulin Sensitivity, Lipid Metabolism and Fat Homeostasis.International journal of molecular sciences · 2022Review
- Inducible expression quantitative trait locus analysis of the MUC5AC gene in asthma in urban populations of children.The Journal of allergy and clinical immunology · 2021Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases.Antioxidants (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
15 authors at 7 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein O-glycosylation is controlled by polypeptide GalNAc-transferases (GalNAc-Ts) that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear. Here we present the first crystal structures of complexes of GalNAc-T2 with glycopeptides that together with enhanced sampling molecular dynamics simulations demonstrate a cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain. Atomic force microscopy and small-angle X-ray scattering experiments further reveal a dynamic conformational landscape of GalNAc-T2 and a prominent role of compact structures that are both required for efficient catalysis. Our model indicates that the activity profile of GalNAc-T2 is dictated by conformational heterogeneity and relies on a flexible linker located between the catalytic and the lectin domains. Our results also shed light on how GalNAc-Ts generate dense decoration of proteins with O-glycans.
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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.