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Sequence requirements of the FFAT‐like motif for specific binding to VAP‐A are revealed by NMR
- Source :
- FEBS Letters. 595:2248-2256
- Publication Year :
- 2021
- Publisher :
- Wiley, 2021.
-
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.
- Subjects :
- Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
Amino Acid Motifs
Vesicular Transport Proteins
Biophysics
Sequence (biology)
Biochemistry
Protein–protein interaction
chemistry.chemical_compound
Structural Biology
RNA polymerase
Genetics
Humans
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
Coronavirus RNA-Dependent RNA Polymerase
SARS-CoV-2
Endoplasmic reticulum
Cell Biology
bacterial infections and mycoses
Transmembrane protein
respiratory tract diseases
Major sperm protein
chemistry
Peptides
Function (biology)
Protein Binding
Subjects
Details
- ISSN :
- 18733468 and 00145793
- Volume :
- 595
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....1be2d5861bea2f972f1f330493bb2b54