Source:http://linkedlifedata.com/resource/pubmed/id/12775711
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
32
|
pubmed:dateCreated |
2003-8-4
|
pubmed:databankReference | |
pubmed:abstractText |
The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chilectins), 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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adipokines,
http://linkedlifedata.com/resource/pubmed/chemical/CHI3L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
8
|
pubmed:volume |
278
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
30206-12
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:12775711-Adipokines,
pubmed-meshheading:12775711-Chondrocytes,
pubmed-meshheading:12775711-Crystallography, X-Ray,
pubmed-meshheading:12775711-Electrons,
pubmed-meshheading:12775711-Glycoproteins,
pubmed-meshheading:12775711-Humans,
pubmed-meshheading:12775711-Lectins,
pubmed-meshheading:12775711-Ligands,
pubmed-meshheading:12775711-Models, Molecular,
pubmed-meshheading:12775711-Oligosaccharides,
pubmed-meshheading:12775711-Protein Binding,
pubmed-meshheading:12775711-Protein Conformation,
pubmed-meshheading:12775711-Signal Transduction
|
pubmed:year |
2003
|
pubmed:articleTitle |
Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.
|
pubmed:affiliation |
Division of Biological Chemistry & Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|