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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-3-9
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pubmed:abstractText |
A number of C5a modifications were tested to determine effects on receptor binding to polymorphonuclear leukocyte (PMNL) membrane receptors and triggering of PMNL chemokinesis and myeloperoxidase (MPO) release. Site-directed mutagenesis was used to probe relationships of key C-terminal residues, and suggested a role for additional sites, particularly Lys19-20. A synthetic peptide based on C5a 19-30, weakly inhibited C5a binding. Potency of the C-terminal octapeptide, a full agonist, was markedly improved by a single Phe substitution for His67, and a Phe point mutation at this site was shown to enhance activity of the full recombinant protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0379-0363
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
17-21
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:1664187-Cells, Cultured,
pubmed-meshheading:1664187-Complement C5a,
pubmed-meshheading:1664187-Humans,
pubmed-meshheading:1664187-Neutrophils,
pubmed-meshheading:1664187-Receptors, Cell Surface,
pubmed-meshheading:1664187-Recombinant Proteins,
pubmed-meshheading:1664187-Structure-Activity Relationship
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pubmed:year |
1991
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pubmed:articleTitle |
C5a structural requirements for neutrophil receptor interaction.
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pubmed:affiliation |
Immunoscience Research Area, Abbott Laboratories, Abbott Park, IL 60064.
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pubmed:publicationType |
Journal Article
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