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

Stawikowska, R, Cudic, M, Giulianotti, M et al. (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. 10.1074/jbc.M113.462267

cited authors

  • Stawikowska, R; Cudic, M; Giulianotti, M; Houghten, RA; Fields, GB; Minond, D

authors

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.

publication date

  • August 2, 2013

published in

Digital Object Identifier (DOI)

start page

  • 22871

end page

  • 22879

volume

  • 288

issue

  • 31