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Structural Basis of Protein-Protein Interactions

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Protein-Protein Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 261))

Abstract

Regulated interactions between proteins govern signaling pathways within and between cells. Although it is possible to derive some general principles of protein-protein recognition from experimentally determined structures, recent structural studies on protein complexes formed during signal transduction illustrate the remarkable diversity of interactions, both in terms of interfacial size and nature. There are two broad classes of complexes: “domain-domain,” in which both components comprise prefolded structural units, and “domain-peptide,” in which one component is a short motif that is unstructured in the absence of its binding partner. Signaling complexes often involve multidomain proteins whose multifaceted binding functions are regulated by intramolecular domain interactions. The structural basis of regulation, via steric and allosteric mechanisms, is discussed.

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Author information

Authors and Affiliations

  1. The Burnham Institute, La Jolla, CA

    Robert C. Liddington

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  1. Robert C. Liddington
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Editor information

Editors and Affiliations

  1. Department of Pharmacology, Emory University School of Medicine, Atlanta, GA

    Haian Fu

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© 2004 Humana Press Inc., Totowa, NJ

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Liddington, R.C. (2004). Structural Basis of Protein-Protein Interactions. In: Fu, H. (eds) Protein-Protein Interactions. Methods in Molecular Biology, vol 261. Humana Press. https://doi.org/10.1385/1-59259-762-9:003

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  • DOI: https://doi.org/10.1385/1-59259-762-9:003

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-120-2

  • Online ISBN: 978-1-59259-762-8

  • eBook Packages: Springer Protocols

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