Engineering allostery into proteins

Scott D. Gorman, Rebecca N. D’Amico, Dennis S. Winston, David D. Boehr

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Our ability to engineer protein structure and function has grown dramatically over recent years. Perhaps the next level in protein design is to develop proteins whose function can be regulated in response to various stimuli, including ligand binding, pH changes, and light. Endeavors toward these goals have tested and expanded on our understanding of protein function and allosteric regulation. In this chapter, we provide examples from different methods for developing new allosterically regulated proteins. These methods range from whole insertion of regulatory domains into new host proteins, to covalent attachment of photoswitches to generate light-responsive proteins, and to targeted changes to specific amino acid residues, especially to residues identified to be important for relaying allosteric information across the protein framework. Many of the examples we discuss have already found practical use in medical and biotechnology applications.

Original languageEnglish (US)
Title of host publicationAdvances in Experimental Medicine and Biology
PublisherSpringer
Pages359-384
Number of pages26
DOIs
StatePublished - Jan 1 2019

Publication series

NameAdvances in Experimental Medicine and Biology
Volume1163
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Gorman, S. D., D’Amico, R. N., Winston, D. S., & Boehr, D. D. (2019). Engineering allostery into proteins. In Advances in Experimental Medicine and Biology (pp. 359-384). (Advances in Experimental Medicine and Biology; Vol. 1163). Springer. https://doi.org/10.1007/978-981-13-8719-7_15