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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2007-6-28
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pubmed:abstractText |
Lectins are proteins of non-immune origin capable of binding saccharide structures with high specificity and affinity. Considering the high encoding capacity of oligosaccharides, this makes lectins important for adhesion and recognition. The present study is devoted to the PA-IIL lectin from Pseudomonas aeruginosa, an opportunistic human pathogen capable of causing lethal complications in cystic fibrosis patients. The lectin may play an important role in the process of virulence, recognizing specific saccharide structures and subsequently allowing the bacteria to adhere to the host cells. It displays high values of affinity towards monosaccharides, especially fucose--a feature caused by unusual binding mode, where two calcium ions participate in the interaction with saccharide. Investigating and understanding the nature of lectin-saccharide interactions holds a great potential of use in the field of drug design, namely the targeting and delivery of active compounds to the proper site of action.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-12415289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-12909014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-14714886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-14969751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15101976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15174156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15463936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15790314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-15870442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-16140523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-16438968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-16768446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-17015462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-2757186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17540045-6808301
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1472-6807
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17540045-Adhesins, Bacterial,
pubmed-meshheading:17540045-Amino Acid Substitution,
pubmed-meshheading:17540045-Binding Sites,
pubmed-meshheading:17540045-Chromatography, Affinity,
pubmed-meshheading:17540045-Crystallography, X-Ray,
pubmed-meshheading:17540045-Lectins,
pubmed-meshheading:17540045-Models, Molecular,
pubmed-meshheading:17540045-Monosaccharides,
pubmed-meshheading:17540045-Mutagenesis, Site-Directed,
pubmed-meshheading:17540045-Plant Lectins,
pubmed-meshheading:17540045-Polymorphism, Single Nucleotide,
pubmed-meshheading:17540045-Protein Conformation,
pubmed-meshheading:17540045-Protein Engineering,
pubmed-meshheading:17540045-Pseudomonas aeruginosa,
pubmed-meshheading:17540045-Ralstonia solanacearum,
pubmed-meshheading:17540045-Recombinant Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference.
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pubmed:affiliation |
National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, Czech Republic. honzadam@chemi.muni.cz <honzadam@chemi.muni.cz>
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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