ArticleBiochemical and biophysical research communications2007
Family 18 chitolectins: comparison of MGP40 and HUMGP39.
Article in Biochemical and biophysical research communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Human Lectins, Their Carbohydrate Affinities and Where to Find Them.Biomolecules · 2021Review
- Inhibition of Mammalian Glycoprotein YKL-40: IDENTIFICATION OF THE PHYSIOLOGICAL LIGAND.The Journal of biological chemistry · 2017Article
- New Insights Into the Relationship Between Chitinase-3-Like-1 and Asthma.Current allergy and asthma reports · 2016Review
- Structure-function analysis of endogenous lectin mind-the-gap in synaptogenesis.Developmental neurobiology · 2012Article
- Analyzing airway inflammation with chemical biology: dissection of acidic mammalian chitinase function with a selective drug-like inhibitor.Chemistry & biology · 2011Article
- YKL-40-A Protein in the Field of Translational Medicine: A Role as a Biomarker in Cancer Patients?Cancers · 2010Article
- Visualisation of cyclic and multi-branched molecules with VMD.Journal of molecular graphics & modelling · 2009Article
- Solid-phase synthesis of cyclic peptide chitinase inhibitors: SAR of the argifin scaffold.Organic & biomolecular chemistry · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Glycosidase and lectins both bind sugars, but only the glycosidases have catalytic activity. The glycosidases occur among over 100 evolved protein families and Family 18 is one of the two chitinases (EC 3, 2.1.14) families. Interestingly, lectins are also in this evolutionary group of Family 18 glycosidase proteins. The proteins belonging to the enzymatically inactive class are referred to as chitolectins and have a binding site that is highly similar to the catalytic Family 18 enzymes. We present a comparison of the recently obtained structures of two Family 18 chitolectins, MGP40 [A.K. Mohanty, G. Singh, M. Paramasivam, K. Saravanan, T. Jabeen, S. Sharma, S. Yadav, P. Kaur, P. Kumar, A. Srinivasan, T.P. Singh, Crystal structure of a novel regulatory 40kDa mammary gland protein (MGP-40) secreted during involution, J. Biol. Chem. 278 (2003) 14451-14460.] and HumGP39 [F. Fusetti, T. Pijning, K.H. Kalk, E. Bos, B.W. Dijkstra, Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39, J. Biol. Chem. 278 (2003) 37753-37760; D.R. Houston, D.R. Anneliese, C.K. Joanne, D.M.V. Aalten, Structure and ligand-induced conformational change of the 39kDa glycoprotein from human articular chondrocytes, J. Biol. Chem. 278 (2003) 30206-30212.] with a focus on the glycosidase active site. We compare the sequence and the structure of these two Family 18 protein classes. The difference between the active and inactive protein is a glutamic acid which acts as the essential acid/base residue for chitin cleavage and is replaced with leucine or glutamine in the chitolectins. Furthermore, a mechanism for the interaction between the chitolectin and oligosaccharides was proposed.
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