High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA
The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we re...
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PeerJ Inc.
2018-03-01
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author | Jonathan R. Davies Gavin S. Hackett Sai Man Liu K. Ravi Acharya |
author_facet | Jonathan R. Davies Gavin S. Hackett Sai Man Liu K. Ravi Acharya |
author_sort | Jonathan R. Davies |
collection | DOAJ |
description | The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production. |
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institution | Directory Open Access Journal |
issn | 2167-8359 |
language | English |
last_indexed | 2024-03-09T08:07:23Z |
publishDate | 2018-03-01 |
publisher | PeerJ Inc. |
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spelling | doaj.art-4220cb3abb9f473c8bdcc9788b5693a22023-12-02T23:45:19ZengPeerJ Inc.PeerJ2167-83592018-03-016e455210.7717/peerj.4552High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FAJonathan R. Davies0Gavin S. Hackett1Sai Man Liu2K. Ravi Acharya3Department of Biology and Biochemistry, University of Bath, Bath, United KingdomIpsen Bioinnovation Limited, Abingdon, United KingdomIpsen Bioinnovation Limited, Abingdon, United KingdomDepartment of Biology and Biochemistry, University of Bath, Bath, United KingdomThe binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production.https://peerj.com/articles/4552.pdfSV2Crystal structureBotulinum neurotoxinTargeted secretion inhibitorFA hybridReceptor binding domain |
spellingShingle | Jonathan R. Davies Gavin S. Hackett Sai Man Liu K. Ravi Acharya High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA PeerJ SV2 Crystal structure Botulinum neurotoxin Targeted secretion inhibitor FA hybrid Receptor binding domain |
title | High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA |
title_full | High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA |
title_fullStr | High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA |
title_full_unstemmed | High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA |
title_short | High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA |
title_sort | high resolution crystal structures of the receptor binding domain of clostridium botulinum neurotoxin serotypes a and fa |
topic | SV2 Crystal structure Botulinum neurotoxin Targeted secretion inhibitor FA hybrid Receptor binding domain |
url | https://peerj.com/articles/4552.pdf |
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