Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes

Douglas R. Houston, Anneliese D. Recklies, Joanne C. Krupa, Daan M F Van Aalten*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chi-lectins), is overexpressed in articular chondrocytes and certain cancers. Proposed functions of this protein include a role in connective tissue remodeling and defense against pathogens. Similar to other Chi-lectins, HCGP39 promotes the growth of connective tissue cells. The ability of HCGP39 to activate cytoplasmic signaling pathways suggests the presence of a ligand for this protein at the cell surface. There is currently no information regarding the identity of any physiological or pathological ligands of the Chi-lectins or the nature of the protein-ligand interaction. Here, we show that HCGP39 is able to bind chitooligosaccharides with micromolar affinity. Crystal structures of the native protein and a complex with GlcNAc8, show that the ligand is bound in identical fashion to family 18 chitinases. However, unlike the chitinases, binding of the oligosaccharide ligand to HCGP39 induces a large conformational change. Thus, HCGP39 could be a lectin that binds chitin-like oligosaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes.

Original languageEnglish
Pages (from-to)30206-30212
Number of pages7
JournalJournal of Biological Chemistry
Issue number32
Publication statusPublished - 8 Aug 2003


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