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Imperfect interfaces

Nature Structural Biology volume 5, pages 412–414 (1998)Cite this article

The crystal structure of a T cell receptor bound to a self peptide–major histocompatibility complex antigen reveals poor shape complementarity in the interface between the two proteins, as well as large conformational changes in the T cell receptor combining site upon ligand binding.

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Author information

Authors and Affiliations

  1. the Center for Drug Evaluation and Research, United States Food and Drug Administration, 5600 Fishers Lane, Rockville, Maryland, 20857, USA

    Xavier Ysern

  2. the Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, Maryland, 20850, USA

    Hongmin Li & Roy A. Mariuzza

Authors
  1. Xavier Ysern
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  2. Hongmin Li
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  3. Roy A. Mariuzza
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Corresponding author

Correspondence to Roy A. Mariuzza.

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Ysern, X., Li, H. & Mariuzza, R. Imperfect interfaces. Nat Struct Mol Biol 5, 412–414 (1998). https://doi.org/10.1038/nsb0698-412

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