Abstract
Protein-protein associations are the basis of much of the macromolecular organization underlying cellular structure and function. Two general mechanisms exist to achieve binding specificity: “surface-surface” and “modular domain-peptide” associations. The former is based on interacting surface chemistry unique to each pair of binding partners, e.g., oligomerization of hemoglobin monomers. Surface-surface interactions provide for highly specific binding, but the complex nature of these associations has not provided evolution with the opportunity to generate binding diversity. In contrast, “modular domain-peptide” associations are based on conserved domains which recognize variations of simple peptide motifs. Both the modular domains and peptide targets are found as motifs within multidomain proteins of diverse function, e.g., enzymes, receptors, cytoskeletal proteins. Examples of these domains include the well characterized SH3, SH2 and PTB domains.
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Fanning, A.S., Anderson, J.M. (1998). PDZ Domains and the Formation of Protein Networks at the Plasma Membrane. In: Pawson, A.J. (eds) Protein Modules in Signal Transduction. Current Topics in Microbiology and Immunology, vol 228. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80481-6_9
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