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Science 31 May 1985:
Vol. 228. no. 4703, pp. 1055 - 1060
DOI: 10.1126/science.3992245
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Articles

Science, Vol 228, Issue 4703, 1055-1060
Copyright © 1985 by American Association for the Advancement of Science

articles

Model structure for the inflammatory protein C5a

J Greer

The complement cleavage product C5a is a potent stimulant of inflammatory processes; thus, inhibition of C5a activity is of therapeutic interest. The three-dimensional structure of the major portion of C5a was modeled from the homologous C3a crystal structure by comparative modeling techniques. The model shows that core residues of C5a are completely conserved, while external residues differ from C3a. Even though the amino-terminal 12 residues of C3a are disordered in the crystal, this sequence in C5a may form an amphipathic helix. The distribution of species sequence differences in the complete C5a structure suggests a possible receptor binding site.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structure-Function Relationships of Human C5a and C5aR.
M. S. Huber-Lang, J. V. Sarma, S. R. McGuire, K. T. Lu, V. A. Padgaonkar, E. M. Younkin, R. F. Guo, C. H. Weber, E. R. Zuiderweg, F. S. Zetoune, et al. (2003)
J. Immunol. 170, 6115-6124
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