ArticleThe Journal of biological chemistry2015
Structural and thermodynamic insights into chitooligosaccharide binding to human cartilage chitinase 3-like protein 2 (CHI3L2 or YKL-39).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Redefining CHI3L1: Therapeutic Opportunities at the Crossroads of Immune Suppression and Disease Progression.Medicinal research reviews · 2026Review
- Chitinase-like proteins de-N-glycosylating CD36 modify cholesterol metabolism in atherosclerotic macrophages.Nature communications · 2026Article
- The emerging role of chitinase-3-like-1 protein in neurodegeneration.Metabolic brain disease · 2025Review
- Structural and functional significance ofJournal of virology · 2025Article
- A Simplified Method for Evaluating Chitin-Binding Activity Applied to YKL-40 (HC-gp39, CHI3L1) and Chitotriosidase.Molecules (Basel, Switzerland) · 2024Article
- Article
- Neuroinflammation and glycosylation-related cerebrospinal fluid proteins for predicting functional decline in amyotrophic lateral sclerosis: a proteomic study.Frontiers in neurology · 2024Article
- Irreversible evolutionary loss of chitin-degrading ability in the chitinase-like protein Ym1 under positive selection in rodents.Protein science : a publication of the Protein Society · 2023Article
- Influence of Association on Binding of Disaccharides to YKL-39 and hHyal-1 Enzymes.International journal of molecular sciences · 2022Article
- CSF Chitinase 3-Like 2 Is Associated With Long-term Disability Progression in Patients With Progressive Multiple Sclerosis.Neurology(R) neuroimmunology & neuroinflammation · 2021Article
- Chitinases and chitinase-like proteins as biomarkers in neurologic disorders.Neurology(R) neuroimmunology & neuroinflammation · 2021Review
- Structural insights into the mechanisms and specificities of IgG-active endoglycosidases.Glycobiology · 2020Review
- Potential mechanisms of action of celastrol against rheumatoid arthritis: Transcriptomic and proteomic analysis.PloS one · 2020Article
- Structural and functional characterization of buffalo oviduct-specific glycoprotein (OVGP1) expressed during estrous cycle.Bioscience reports · 2019Article
- Distinct degenerative phenotype of articular cartilage from knees with meniscus tear compared to knees with osteoarthritis.Osteoarthritis and cartilage · 2019Article
- Molecular Basis of Broad SpectrumACS central science · 2019Article
- YKL-39 as a Potential New Target for Anti-Angiogenic Therapy in Cancer.Frontiers in immunology · 2019Review
- Anti-inflammatory effects in a mouse osteoarthritis model of a mixture of glucosamine and chitooligosaccharides produced by bi-enzyme single-step hydrolysis.Scientific reports · 2018Article
- Functional analysis of an unusual porin-like channel that imports chitin for alternative carbon metabolism inThe Journal of biological chemistry · 2017Article
- YKL-40/chitinase-3-like protein 1 is associated with poor prognosis and promotes cell growth and migration of cholangiocarcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Four crystal structures of human YKL-39 were solved in the absence and presence of chitooligosaccharides. The structure of YKL-39 comprises a major (β/α)8 triose-phosphate isomerase barrel domain and a small α + β insertion domain. Structural analysis demonstrates that YKL-39 interacts with chitooligosaccharides through hydrogen bonds and hydrophobic interactions. The binding of chitin fragments induces local conformational changes that facilitate tight binding. Compared with other GH-18 members, YKL-39 has the least extended chitin-binding cleft, containing five subsites for sugars, namely (-3)(-2)(-1)(+1)(+2), with Trp-360 playing a prominent role in the sugar-protein interactions at the center of the chitin-binding cleft. Evaluation of binding affinities obtained from isothermal titration calorimetry and intrinsic fluorescence spectroscopy suggests that YKL-39 binds to chitooligosaccharides with Kd values in the micromolar concentration range and that the binding energies increase with the chain length. There were no significant differences between the Kd values of chitopentaose and chitohexaose, supporting the structural evidence for the five binding subsite topology. Thermodynamic analysis indicates that binding of chitooligosaccharide to YKL-39 is mainly driven by enthalpy.
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