Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates

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Abstract

Background: Structural determinants of ADAM17 substrate specificity are unknown. Results: ADAM17 activity affected by noncatalytic domains and secondary structure of substrates. Conclusion: Noncatalytic domains and substrate conformation are potentially the key structural elements that determine ADAM17 specificity. Significance: Understanding interaction of ADAM17 with its substrates will assist in discoveryADAMisoform-and substratespecific inhibitors. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Stawikowska, R., Cudic, M., Giulianotti, M., Houghten, R. A., Fields, G. B., & Minond, D. (2013). Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates. Journal of Biological Chemistry, 288(31), 22871–22879. https://doi.org/10.1074/jbc.M113.462267

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