Notch Transmembrane Domain: Secondary Structure and Topology | Zendy

Catherine L. Deatherage | Zendy; Zhenwei Lu | Zendy; Ji Hun Kim | Zendy; Charles R. Sanders | Zendy

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Notch Transmembrane Domain: Secondary Structure and Topology

Author(s) -

Catherine L. Deatherage,

Zhenwei Lu,

Ji Hun Kim,

Charles R. Sanders

Publication year - 2015

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/acs.biochem.5b00456

Subject(s) - transmembrane domain , transmembrane protein , notch signaling pathway , cleavage (geology) , microbiology and biotechnology , chemistry , domain (mathematical analysis) , obligate , membrane topology , function (biology) , biophysics , topology (electrical circuits) , signal transduction , biology , membrane , biochemistry , receptor , paleontology , mathematical analysis , mathematics , combinatorics , fracture (geology) , ecology

The Notch signaling pathway is critical in development, neuronal maintenance, and hematopoiesis. An obligate step in the activation of this pathway is cleavage of its transmembrane (TM) domain by γ-secretase. While the soluble domains have been extensively studied, little has been done to characterize its TM and flanking juxtamembrane (JM) segments. Here, we present the results of nuclear magnetic resonance (NMR) studies of the human Notch1 TM/JM domain. The TM domain is largely α-helical. While the flanking JM segments do not adopt regular secondary structure, they interact with the membrane surface, suggesting membrane interactions may play a role in modulating its cleavage by γ-secretase and subsequent NOTCH signaling function.

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