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Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme

Nature Structural Biology volume 3, pages 803–811 (1996)Cite this article

Abstract

The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies, lacking light chains. We report here the 2.5 Å resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mouse VH domains, there are no major backbone rearrangements in the VH framework. However, the architecture of the region of VH that interacts with a VL in a conventional Fv is different from any previously seen. Moreover, the CDR1 region, although in sequence homologous to human CDR1, deviates fundamentally from the canonical structure. Additionally, one half of the CDR3 contacts the VH region which in conventional immunoglobulins interacts with a VL, whereas the other half protrudes from the antigen binding site and penetrates deeply into the active site of lysozyme.

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Authors and Affiliations

  1. Department Ultrastructure, Vlaams Interuniversitair Instituutvoor Biotechnologie, Vrije Universiteit, Brussel Paardenstraat 65, B-1640, Sint Genesius Rode, Belgium

    Aline Desmyter, Thomas R. Transue, Mehdi Arbabi Ghahroudi, Minh-Hoa Dao Thi, Serge Muyldermans & Lode Wyns

  2. Department Algemene Biologie, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640, Sint Genesius Rode, Belgium

    Raymond Hamers

  3. Vlaamse Instelling voor Technologisch Onderzoek, Boeretang, 200, B-2400, Mol, Belgium

    Freddy Poortmans

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Desmyter, A., Transue, T., Ghahroudi, M. et al. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme. Nat Struct Mol Biol 3, 803–811 (1996). https://doi.org/10.1038/nsb0996-803

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