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The crystal structure of a llama heavy chain variable domain

Nature Structural Biology volume 3, pages 752–757 (1996)Cite this article

The 1.85 Å structure of an antigen-free llama heavy chain variable domain reveals a fold similarity to that of the classical immunoglobulin VHs, increased surface hydrophilicity of the side of the VH corresponding to that facing the VL domain in classical immunoglobulins, and alterations in the pattern of the CDRs.

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Authors and Affiliations

  1. Architecture et Fonction des Macromolécules Biologiques, CNRS UPR 9039, 31, Chemin Joseph Aiguier, 13402, Marseille, Cedex 20, France

    Silvia Spinelli, Christelle Anguille, Christian Cambillau & Marietta Tegonil

  2. Unilever Research Laboratorium, Olivier van Noortlaan 120, 3133 AT, Vlaardingen, The Netherlands

    Leon Frenken, Lian de Ron, Will Bos & Theo Verrips

  3. European Synchrotron Radiation Facility, BP 220, 38043, Grenoble, France

    Dominique Bourgeois

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  1. Silvia Spinelli
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Spinelli, S., Frenken, L., Bourgeois, D. et al. The crystal structure of a llama heavy chain variable domain. Nat Struct Mol Biol 3, 752–757 (1996). https://doi.org/10.1038/nsb0996-752

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