Sequence requirements of the FFAT-like motif for specific binding to VAP-A are revealed by NMR.
FEBS Lett
; 595(17): 2248-2256, 2021 09.
Article
in English
| MEDLINE | ID: covidwho-1326724
ABSTRACT
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-AMSP ) 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-AMSP as well as other FFAT-like motifs. Our results will contribute to the discovery of new VAP interactors.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Peptides
/
Vesicular Transport Proteins
/
Coronavirus RNA-Dependent RNA Polymerase
/
SARS-CoV-2
Limits:
Humans
Language:
English
Journal:
FEBS Lett
Year:
2021
Document Type:
Article
Affiliation country:
1873-3468.14166
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