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NMR Studies of the Structure and Role of Modules Involved in Protein-Protein Interactions

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Book cover NMR of Proteins

Part of the book series: Topics in Molecular and Structural Biology ((TMSB))

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Abstract

Non-covalent molecular interactions in biological systems are ubiquitous and finely tuned. While enzyme substrate complexes are relatively well understood and considerable knowledge has been gained recently about the way proteins interact with DNA (Harrison, 1991), understanding of protein-protein interactions is relatively poor. Many complexes involving proteins are large and apparently intractable for structural studies. Examples of interest include: cell-cell interactions mediated by different adhesion molecules; a cytokine bound to a membrane receptor; a tyrosine kinase bound to a protein substrate; a blood clotting complex. In cases where there is information available about protein-protein interactions, e.g. in antibody/protein antigen complexes, the interacting protein surface patches seem to involve more than one peptide loop from different parts of the protein sequence (Chothia, 1991).

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Authors
  1. Iain D. Campbell
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  2. Paul C. Driscoll
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Editors and Affiliations

  1. Laboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA

    G. M. Clore  & A. M. Gronenborn  & 

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Campbell, I.D., Driscoll, P.C. (1993). NMR Studies of the Structure and Role of Modules Involved in Protein-Protein Interactions. In: Clore, G.M., Gronenborn, A.M. (eds) NMR of Proteins. Topics in Molecular and Structural Biology. Palgrave, London. https://doi.org/10.1007/978-1-349-12749-8_5

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  • DOI: https://doi.org/10.1007/978-1-349-12749-8_5

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