FEBS Letters | |
Sequence requirements of the FFAT-like motif for specific binding to VAP-A are revealed by NMR | |
article | |
Kyoko Furuita1  Marina Hiraoka2  Kentaro Hanada3  Toshimichi Fujiwara1  Chojiro Kojima1  | |
[1] Institute for Protein Research, Osaka University;Graduate School of Engineering Science, Yokohama National University;Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases | |
关键词: FFAT motif; FFAT-like motif; protein–protein interaction; SARS-CoV-2; solution NMR; VAMP-associated protein; | |
DOI : 10.1002/1873-3468.14166 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The endoplasmic reticulum transmembrane protein vesicle-associated membrane protein-associated protein (VAP) plays a central role in the formation and function of membrane contact sites (MCS) through its interactions with proteins. The major sperm protein (MSP) domain of VAP binds to a variety of sequences which are referred to as FFAT-like motifs. In this study, we investigated the interactions of eight peptides containing FFAT-like motifs with the VAP-A MSP domain (VAP-A MSP ) by solution NMR. Six of eight peptides are specifically bound to VAP-A. Furthermore, we found that the RNA-dependent RNA polymerase of severe acute respiratory syndrome coronavirus 2 has an FFAT-like motif which specifically binds to VAP-A MSP as well as other FFAT-like motifs. Our results will contribute to the discovery of new VAP interactors.
【 授权许可】
Unknown
【 预 览 】
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RO202302050002098ZK.pdf | 2217KB | download |