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The H3 loop of antibodies shows unique structural characteristics

Abstract:

The H3 loop in the Complementary Determining Region (CDR) of antibodies plays a key role in their ability to bind the diverse space of potential antigens. It is also exceptionally difficult to model computationally causing a significant hurdle for in-silico development of antibody biotherapeutics. In this paper we show that most H3s have unique structural characteristics which may explain why they are so challenging to model. We found that over 75% of H3 loops do not have a sub-Angstrom st...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1002/prot.25291

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Department:
Oxford, MPLS, Statistics
Role:
Author
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Department:
Kellogg College
Role:
Author
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Grant:
Systems Approaches and Biomedical Sciences Center for Doctoral Training (Grant EP/G037280/1)
MedImmune Ltd More from this funder
Publisher:
Wiley Publisher's website
Journal:
Proteins: Structure, Function, and Bioinformatics Journal website
Volume:
85
Issue:
7
Pages:
1311–1318
Publication date:
2017-01-01
Acceptance date:
2017-03-18
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
Pubs id:
pubs:686666
URN:
uri:a64f36e8-740a-435b-801f-139720c920fb
UUID:
uuid:a64f36e8-740a-435b-801f-139720c920fb
Local pid:
pubs:686666
Paper number:
7

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