Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29

Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29

VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from Zn-fingers and further show that mutations, which...

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Bibliographic Details
Main Authors: Harriet Crawley-Snowdon, Ji-Chun Yang, Nathan R. Zaccai, Luther J. Davis, Lena Wartosch, Emily K. Herman, Nicholas A. Bright, James S. Swarbrick, Brett M. Collins, Lauren P. Jackson, Matthew N. J. Seaman, J. Paul Luzio, Joel B. Dacks, David Neuhaus, David J. Owen
Format: Article
Language:English
Published: Nature Portfolio 2020-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-18773-2

Internet

https://doi.org/10.1038/s41467-020-18773-2

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