Assembling an ion channel: ORF 3a from SARS‐CoV
Identifieur interne : 000294 ( Istex/Curation ); précédent : 000293; suivant : 000295Assembling an ion channel: ORF 3a from SARS‐CoV
Auteurs : Tze-Hsiang Chien [Taïwan] ; Ya-Ling Chiang [Taïwan] ; Chin-Pei Chen [Taïwan] ; Petra Henklein [Allemagne] ; Karen H Nel [Allemagne] ; Ing-Shouh Hwang [Taïwan] ; Dieter Willbold [Allemagne] ; Wolfgang B. Fischer [Taïwan]Source :
- Biopolymers [ 0006-3525 ] ; 2013-09.
English descriptors
- Teeft :
- A_id, Amino acids, Assembly process, Bilayer, Bilayer recordings, Biochim biophys acta, Biol, Biol chem, Biophys, Biopolymers, Buffer conditions, Cadmus, Calcium buffer, Channel, Channel activity, Channel protein, Channel recording data, Channel recordings, Chem, Conductance, Conductance levels, Conductance patterns, Conductance states, Contract grant sponsor, Customer a_id, Experimental data, Febs lett, Fischer, Full length, Full length protein, Fusion protein, Gating kinetics, Individual tmds, J_id, Linear regression analysis, Lipid, Lipid bilayer, Lipid bilayers, Lipid membrane, Lipid membranes, Manoharj, Manoharj time, Middle panel, Monomer, Negative voltages, Nicotinic acetylcholine, Peptide, Polytopic channel proteins, Pore, Positive voltage, Potassium buffer, Potassium channel, Potassium ions, Present study, Proc natl acad, Protein expression, Reconstituted, Room temperature, Selectivity, Stock solution, Tetrameric channel, Tmd1, Tmd2, Tmd3, Tmds, Viral channel, Wang, Weight ratio, Wiley periodicals.
Abstract
Protein 3a is a 274 amino acid polytopic channel protein with three putative transmembrane domains (TMDs) encoded by severe acute respiratory syndrome corona virus (SARS‐CoV). Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. Biopolymers 99:628–635, 2013.
Url:
DOI: 10.1002/bip.22230
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Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. Biopolymers 99:628–635, 2013.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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