Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB

Appu K. Singh; Kei Saotome; Luke L. McGoldrick; Alexander I. Sobolevsky

doi:10.1038/s41467-018-04828-y

Nature Communications (Jun 2018)

Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB

Appu K. Singh,
Kei Saotome,
Luke L. McGoldrick,
Alexander I. Sobolevsky

Affiliations

Appu K. Singh: Department of Biochemistry and Molecular Biophysics, Columbia University
Kei Saotome: Department of Biochemistry and Molecular Biophysics, Columbia University
Luke L. McGoldrick: Department of Biochemistry and Molecular Biophysics, Columbia University
Alexander I. Sobolevsky: Department of Biochemistry and Molecular Biophysics, Columbia University

DOI: https://doi.org/10.1038/s41467-018-04828-y
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 11

Abstract

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The transient receptor potential channel TRPV6 mediates calcium uptake in epithelia and its expression is increased in several cancer types. Here, authors present structures of TRPV6 bound to 2-APB, a TRPV6 inhibitor, and show that 2-APB induces TRPV6 channel closure by modulating protein–lipid interactions.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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