NDLI: The pharmacophore of the human C5a anaphylatoxin.

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The pharmacophore of the human C5a anaphylatoxin.

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The pharmacophore of the human C5a anaphylatoxin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Galakatos, N. Braunwalder, A. F. Seligmann, B. Huwyler, L. Yarwood, D. Haston, W. O. Sills, M. A. Hadala, J. Toth, M. J. Boyar, W. C.
Description	Author Affiliation: Toth MJ ( Department of Biological Technologies, Ciba-Geigy Corporation, Summit, New Jersey 07901.)
Abstract	We have determined which amino acids contribute to the pharmacophore of human C5a, a potent inflammatory mediator. A systematic mutational analysis of this 74-amino acid protein was performed and the effects on the potency of receptor binding and of C5a-induced intracellular calcium ion mobilization were measured. This analysis included the construction of hybrids between C5a and the homologous but unreactive C3a protein and site-directed mutagenesis. Ten noncontiguous amino acids from the structurally well-defined 4-helix core domain (amino acids 1-63) and the C-terminal arginine-containing tripeptide were found to contribute to the pharmacophore of human C5a. The 10 mostly charged amino acids from the core domain generally made small incremental contributions toward binding affinity, some of which were independent. Substitutions of the C-terminal amino acid Arg 74 produced the largest single effect. We also found the connection between these 2 important regions to be unconstrained.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	8
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Complement C5a Chemistry Pharmacology Alanine Amino Acid Sequence Binding, Competitive Calcium Metabolism Cell Membrane Complement C3a Genetics Molecular Sequence Data Mutagenesis, Site-directed Neutrophils Point Mutation Protein Structure, Secondary Recombinant Fusion Proteins Structure-activity Relationship Thermodynamics Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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