pubmed-article:16514117 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16514117 | lifeskim:mentions | umls-concept:C0084692 | lld:lifeskim |
pubmed-article:16514117 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
pubmed-article:16514117 | lifeskim:mentions | umls-concept:C1148582 | lld:lifeskim |
pubmed-article:16514117 | lifeskim:mentions | umls-concept:C0178849 | lld:lifeskim |
pubmed-article:16514117 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:16514117 | pubmed:dateCreated | 2006-6-19 | lld:pubmed |
pubmed-article:16514117 | pubmed:abstractText | Interactions of surfactant protein D (SP-D) with micro-organisms and organic antigens involve binding to the trimeric neck plus carbohydrate recognition domain (neck+CRD). In these studies, we compared the ligand binding of homologous human, rat, and mouse trimeric neck+CRD fusion proteins, each with identical N-terminal tags remote from the ligand-binding surface. Although rat and mouse showed similar affinities for saccharide competitors, both differed markedly from the human protein. The human neck+CRD preferentially recognized N-acetyl-mannosamine, whereas the rat and mouse proteins showed greater affinity for myoinositol, maltose, and glucose. Although human neck+CRDs bound to maltosyl-agarose and fungal mannan, only rat and mouse neck+CRDs showed significant binding to maltosyl-Toyopearl beads, solid-phase maltosyl-albumin neo-glycoprotein, or the Phil82 strain of influenza A virus. Likewise, human SP-D dodecamers and trimeric subunits of full-length rat, but not full-length human SP-D trimers, bound to maltosyl-Toyopearl. Site-directed mutagenesis of the human neck+CRD demonstrated an important role of Asp324-Asp325 in the recognition of N-acetyl-mannosamine, and substitution of the corresponding murine sequence (Asn324-Asn325) conferred a capacity to interact with immobilized maltose. Thus, ligand recognition by human SP-D involves a complex interplay between saccharide presentation, the valency of trimeric subunits, and species-specific residues that flank the primary carbohydrate binding site. | lld:pubmed |
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pubmed-article:16514117 | pubmed:language | eng | lld:pubmed |
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pubmed-article:16514117 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16514117 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16514117 | pubmed:month | Jul | lld:pubmed |
pubmed-article:16514117 | pubmed:issn | 1044-1549 | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:HartshornKeva... | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:SmithKellyK | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:CrouchErika... | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:HolmskovUffeU | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:BrinerDavidD | lld:pubmed |
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pubmed-article:16514117 | pubmed:author | pubmed-author:HeadJamesJ | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:LindersBruceB | lld:pubmed |
pubmed-article:16514117 | pubmed:author | pubmed-author:McDonaldJosep... | lld:pubmed |
pubmed-article:16514117 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16514117 | pubmed:volume | 35 | lld:pubmed |
pubmed-article:16514117 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16514117 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16514117 | pubmed:pagination | 84-94 | lld:pubmed |
pubmed-article:16514117 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:16514117 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16514117 | pubmed:articleTitle | Species differences in the carbohydrate binding preferences of surfactant protein D. | lld:pubmed |
pubmed-article:16514117 | pubmed:affiliation | Dept. of Pathology and Immunology, Campus Box 8118, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA. crouch@path.wustl.edu | lld:pubmed |
pubmed-article:16514117 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16514117 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16514117 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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