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The allosteric modulation of Complement C5 by knob domain peptides

Abstract:

Bovines have evolved a subset of antibodies with ultra-long CDRH3 regions that harbour cysteine-rich knob domains. To produce high affinity peptides, we previously isolated autonomous 3-6 kDa knob domains from bovine antibodies. Here, we show that binding of four knob domain peptides elicits a range of effects on the clinically validated drug target complement C5. Allosteric mechanisms predominated, with one peptide selectively inhibiting C5 cleavage by the alternative pathway C5 convertase, ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.7554/eLife.63586

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Role:
Author
ORCID:
0000-0002-4508-5322
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Role:
Author
ORCID:
0000-0002-8425-3704
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Role:
Author
ORCID:
0000-0002-4495-8689
Publisher:
eLife Sciences Publications
Journal:
eLife More from this journal
Volume:
10
Article number:
e63586
Publication date:
2021-03-18
Acceptance date:
2021-02-11
DOI:
EISSN:
2050-084X
Pmid:
33570492
Language:
English
Keywords:
Pubs id:
1161491
Local pid:
pubs:1161491
Deposit date:
2021-03-16

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