Source:http://linkedlifedata.com/resource/pubmed/id/18272393
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-3-26
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pubmed:abstractText |
The Atlantic salmon C-type lectin receptor C (SCLRC) locus encodes a potential oligomeric type II receptor. C-type lectins recognize carbohydrates in a Ca(2+)-dependent manner through structurally conserved, yet functionally diverse, C-type lectin-like domains (CTLDs). Many conserved amino acids in animal CTLDs are present in SCLRC, with the notable exception of an asparagine crucially involved in Ca(2+)- and carbohydrate-binding, which is tyrosine in SCLRC. SCLRC also contains six cysteines that form three disulfide bonds. Although SCLRC was originally identified as an up-regulated transcript responding to Aeromonas salmonicida infection, the biological role of this protein is still unknown. To study the structure and ligand binding properties of SCLRC, we created a homology model of the 17kDa CTLD and produced it as an affinity-tagged protein in the periplasm of Escherichia coli by co-expression of proteins that facilitate disulfide bond formation. The recombinant form of SCLRC was characterized by a protease protection assay, a solid-phase carbohydrate-binding assay, and frontal affinity chromatography. On the basis of this characterization, we classify SCLRC as a C-type lectin that binds to mannose and its derivatives.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1096-0279
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
38-46
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pubmed:meshHeading |
pubmed-meshheading:18272393-Amino Acid Sequence,
pubmed-meshheading:18272393-Animals,
pubmed-meshheading:18272393-Base Sequence,
pubmed-meshheading:18272393-Calcium,
pubmed-meshheading:18272393-Chromatography, Affinity,
pubmed-meshheading:18272393-Escherichia coli,
pubmed-meshheading:18272393-Galactose,
pubmed-meshheading:18272393-Lectins, C-Type,
pubmed-meshheading:18272393-Mannose,
pubmed-meshheading:18272393-Models, Molecular,
pubmed-meshheading:18272393-Molecular Sequence Data,
pubmed-meshheading:18272393-Protein Structure, Tertiary,
pubmed-meshheading:18272393-Recombinant Proteins,
pubmed-meshheading:18272393-Salmo salar,
pubmed-meshheading:18272393-Sequence Alignment,
pubmed-meshheading:18272393-Trypsin
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pubmed:year |
2008
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pubmed:articleTitle |
Recombinant production and characterization of the carbohydrate recognition domain from Atlantic salmon C-type lectin receptor C (SCLRC).
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pubmed:affiliation |
NRC Institute for Marine Biosciences, National Research Council Canada, 1411 Oxford Street, Halifax, NS, Canada B3H 3Z1.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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