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PubMed · 1664187

C5a structural requirements for neutrophil receptor interaction.

K W Mollison·T A Fey·R A Krause·L Miller·R P Edalji·R G Conway·W Mandecki·M A Shallcross·M Kawai·Y S Or
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Abstract

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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Cells, CulturedComplement C5aHumansNeutrophilsReceptors, Cell SurfaceRecombinant ProteinsStructure-Activity RelationshipJournal Article

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K W Mollison, T A Fey, R A Krause, L Miller, R P Edalji, R G Conway, W Mandecki, M A Shallcross, M Kawai, Y S Or. 1991. C5a structural requirements for neutrophil receptor interaction.. https://pubmed.ncbi.nlm.nih.gov/1664187/

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