Nuclear Magnetic Resonance Structural Mapping Reveals Promiscuous Interactions between Clathrin-Box Motif Sequences and the N-Terminal Domain of the Clathrin Heavy Chain
Author:
Affiliation:
1. Department of Biochemistry and Center for Biomedical Neuroscience, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, United States
Funder
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00065
Reference34 articles.
1. Molecular mechanism and physiological functions of clathrin-mediated endocytosis
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4. Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain β-propeller
5. Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking
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