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Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
- Source :
- Journal of Biological Chemistry
- Publication Year :
- 2014
- Publisher :
- Elsevier BV, 2014.
-
Abstract
- Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations. Accepted version
- Subjects :
- Models, Molecular
Conformational change
Viral protein
viruses
Molecular Sequence Data
Golgi Apparatus
Biology
medicine.disease_cause
Biochemistry
Protein Structure, Secondary
Viroporin Proteins
Protein structure
Viral Envelope Proteins
Spectroscopy, Fourier Transform Infrared
Escherichia coli
medicine
Humans
Amino Acid Sequence
Molecular Biology
Peptide sequence
Coronavirus
Binding Sites
Sequence Homology, Amino Acid
Circular Dichroism
virus diseases
Golgi Targeting
Cell Biology
Recombinant Proteins
Transmembrane protein
Science::Biological sciences [DRNTU]
respiratory tract diseases
Protein Structure, Tertiary
Crystallography
Severe acute respiratory syndrome-related coronavirus
Structural biology
Protein Structure and Folding
Mutation
Biophysics
Electrophoresis, Polyacrylamide Gel
Protein Multimerization
Signal Transduction
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 289
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....89bf54628162b0ef82211011b8e06e98