Martin, ACR; (2016) The structural basis of protein moonlighting. In: Henderson, B and Fares, MA and Martin, ACR, (eds.) Protein Moonlighting in Biology and Medicine. (pp. 45-61). John Wiley and Sons, Inc: London, UK.

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Abstract

This chapter reviews some of the basics of protein structure and function and the nature of protein moonlighting. It discusses a few mechanisms of protein moonlighting in detail from a structural perspective. Historically, one of the first examples of proteins being found to have a secondary function was the discovery that eye lens crystallins are often core metabolic enzymes. Whether one considers catalytic promiscuity to be a form of moonlighting depends on one's threshold for functions to be unrelated; consequently catalytic promiscuity is often regarded as a borderline class of moonlighting. From a structural perspective, exploiting separate functional sites is a quite different phenomenon from catalytic promiscuity. It is possible for proteins to demonstrate moonlighting functions through differences in the way in which they associate, forming monomers or other oligomers. Similarly, proteins such as antibodies have separate domains with distinct functions, and these functions are different aspects of the same overall purpose of the protein.

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