Journal article
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
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Authors
Funding
+ Engineering and Physical Sciences Research Council
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Grant:
SystemsApproaches
BiomedicalSciencesCenterforDoctoralTraining(GrantEP/G037280/1
Roche GmbH
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MedImmune Ltd
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UCB Pharma
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Bibliographic Details
- 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
Item Description
- Keywords:
- Pubs id:
-
pubs:686666
- UUID:
-
uuid:a64f36e8-740a-435b-801f-139720c920fb
- Local pid:
- pubs:686666
- Source identifiers:
-
686666
- Deposit date:
- 2017-03-22
Terms of use
- Copyright holder:
- Regep et al
- Copyright date:
- 2017
- Notes:
-
Copyright © 2017 The Authors. Proteins: Structure, Function and Bioinformatics Published by Wiley Periodicals, Inc.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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