Notch Transmembrane Domain: Secondary Structure and Topology.

Deatherage CL, Lu Z, Kim JH, Sanders CR
Biochemistry. 2015 54 (23): 3565-8

PMID: 26023825 · PMCID: PMC4472088 · DOI:10.1021/acs.biochem.5b00456

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.

MeSH Terms (13)

Humans Lipid Bilayers Lysophosphatidylcholines Models, Molecular Nuclear Magnetic Resonance, Biomolecular Peptide Fragments Phosphatidylcholines Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Receptor, Notch1 Recombinant Proteins Surface Properties

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