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pubmed-article:1664187pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:1664187pubmed:dateRevised2005-11-17lld:pubmed
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pubmed-article:1664187pubmed:articleTitleC5a structural requirements for neutrophil receptor interaction.lld:pubmed
pubmed-article:1664187pubmed:affiliationImmunoscience Research Area, Abbott Laboratories, Abbott Park, IL 60064.lld:pubmed
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