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Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):190-7. doi: 10.1107/S0907444909049051. Epub 2010 Jan 22.

Structure of human desArg-C5a.

Author information

1
University of Alabama at Birmingham, Birmingham, AL 35294, USA. wjcook@uab.edu

Abstract

The anaphylatoxin C5a is derived from the complement component C5 during activation of the complement cascade. It is an important component in the pathogenesis of a number of inflammatory diseases. NMR structures of human and porcine C5a have been reported; these revealed a four-helix bundle stabilized by three disulfide bonds. The crystal structure of human desArg-C5a has now been determined in two crystal forms. Surprisingly, the protein crystallizes as a dimer and each monomer in the dimer has a three-helix core instead of the four-helix bundle noted in the NMR structure determinations. Furthermore, the N-terminal helices of the two monomers occupy different positions relative to the three-helix core and are completely different from the NMR structures. The physiological significance of these structural differences is unknown.

PMID:
20124699
DOI:
10.1107/S0907444909049051
[Indexed for MEDLINE]

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