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Structure of and influence of a tick complement inhibitor on human complement component 5.

Abstract:

To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A. The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved. However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5. Binding of the tick C5 inhibitor OmC...

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Publication status:
Published

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Publisher copy:
10.1038/ni.1625

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
Nature immunology More from this journal
Volume:
9
Issue:
7
Pages:
753-760
Publication date:
2008-07-01
DOI:
EISSN:
1529-2916
ISSN:
1529-2908
Language:
English
Keywords:
Pubs id:
pubs:24006
UUID:
uuid:f92209b9-a46d-4888-8c2b-f58c429fc71c
Local pid:
pubs:24006
Source identifiers:
24006
Deposit date:
2012-12-19

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