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

Roma Stawikowska; Mare Cudic; Marc Giulianotti; Richard A. Houghten; Gregg B. Fields; Dmitriy Minond

doi:10.1074/jbc.M113.462267

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

Roma Stawikowska, Mare Cudic, Marc Giulianotti, Richard A. Houghten, Gregg B. Fields, Dmitriy Minond

Research output: Contribution to journal › Article › peer-review

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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.

Original language	English (US)
Pages (from-to)	22871-22879
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M113.462267
State	Published - Aug 2 2013
Externally published	Yes

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10.1074/jbc.M113.462267

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

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.",

author = "Roma Stawikowska and Mare Cudic and Marc Giulianotti and Houghten, {Richard A.} and Fields, {Gregg B.} and Dmitriy Minond",

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doi = "10.1074/jbc.M113.462267",

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AU - Stawikowska, Roma

AU - Cudic, Mare

AU - Giulianotti, Marc

AU - Houghten, Richard A.

AU - Fields, Gregg B.

AU - Minond, Dmitriy

PY - 2013/8/2

Y1 - 2013/8/2

N2 - 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.

AB - 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.

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 31

ER -

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

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