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Structure of and influence of a tick complement inhibitor on human complement component 5 (vol 9, pg 753, 2008)

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 Å. 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

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
NATURE IMMUNOLOGY
Volume:
9
Issue:
7
Pages:
753-760
Publication date:
2008-07-01
DOI:
EISSN:
1529-2916
ISSN:
1529-2908
Language:
English
Pubs id:
pubs:3139
UUID:
uuid:07ff5152-5302-4736-bae8-8c7bf48a1144
Local pid:
pubs:3139
Source identifiers:
3139
Deposit date:
2012-12-19

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