CovidV2, Main, Exploration, bibRecord, 001287

Assembling viral channel forming proteins: Vpu from HIV‐1

Identifieur interne : 001287 ( Main/Exploration ); précédent : 001286; suivant : 001288

Assembling viral channel forming proteins: Vpu from HIV‐1

Auteurs : Li-Hua Li [Taïwan] ; Hao-Jen Hsu [Taïwan] ; Wolfgang B. Fischer [Taïwan]

Source :

Biopolymers [ 0006-3525 ] ; 2013-08.

RBID : ISTEX:EADC15C880C35DDA8987342F328827E85AA5AF2E

English descriptors

Teeft :
- Alanine, Amino acids, Assembly protocol, Bilayer, Biochim biophys acta, Biol chem, Biomol struct, Biophys, Biopolymers, Bundle structure, Cell host microbe, Central axis, Chem, Computational, Conformational space, Dark spheres, Different routes, Dimer, Docking approach, Energy plots, Energy structure, Energy structures, Energy valleys, Energy values, Experimental evidence, Feb, Febs lett, Fischer, Fischer figure, Fischer table, Graphical representation, Handedness, Head group region, Helix, Hydrogen atoms, Hydrophilic residues, Hydrophobic residues, Individual helices, Information figure, Interhelical distance, Kink, Kink angles, Lett, Lipid, Lipid membrane, Lipid molecules, Lipid patch, Lower panels, Lowest energy structure, Lowest energy structures, Lowest structure, Lowest structures, Multiple assembly states, National center, Oxygen atoms, Pentamer, Pentameric, Pentameric assemblies, Pentameric assembly, Pentameric bundles, Peptide, Phosphate atoms, Pore, Proc natl acad, Protocol, Rmsd, Rmsd values, Rmsf, Rmsf values, Rotational, Rotational angle, Rotational angles, Sequential, Sequential assembly, Serine, Simulation, Simultaneous assembly protocol, Strebel, Structural information, Structural integrity, Structural models, Terminal side, Tetramer, Tetrameric, Tetrameric bundles, Tilt angles, Trimer, Tryptophan, Viral, Viral channel, Virol, Water molecules, Wiley periodicals.

Abstract

Different routes of assembly are probed for the transmembrane domain (TMD) of the bitopic membrane protein Vpu from HIV‐1. Vpu is responsible for the amplification of viral release from the host cell. The mode of action includes (i) heteroassembly with host factors and (ii) the formation of homo‐oligomers, which are able to conduct ions across the lipid membrane. Two different routes of assembling short sequences of the N terminus, including the TMD of Vpu, Vpu1–32, and Vpu8–26, are presented by using a combination of classical molecular dynamics (MD) simulations combined with a docking approach. The rim of alanines (Ala‐8, ‐11, ‐15, and ‐19) resembles an interlocking motif for the sequential assembly into a dimer and trimer. Simultaneous assembly results in oligomeric bundles (trimers to pentamers) with either tryptophans (Trp‐23) or purely hydrophobic residues facing the center. Bundles, with serines facing the pore (Ser‐24), are energetically not the lowest structures. For pentameric bundles with Ser‐24 facing the pore, no water column develops during a short 25 ns MD simulation. © 2013 Wiley Periodicals, Inc. Biopolymers 99: 517–529, 2013.

Url:

https://api.istex.fr/ark:/67375/WNG-9JM2H7DW-H/fulltext.pdf

DOI: 10.1002/bip.22210

Affiliations:

Taïwan

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Le document en format XML

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<term>Rotational angle</term>
<term>Rotational angles</term>
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<term>Structural models</term>
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<front><div type="abstract">Different routes of assembly are probed for the transmembrane domain (TMD) of the bitopic membrane protein Vpu from HIV‐1. Vpu is responsible for the amplification of viral release from the host cell. The mode of action includes (i) heteroassembly with host factors and (ii) the formation of homo‐oligomers, which are able to conduct ions across the lipid membrane. Two different routes of assembling short sequences of the N terminus, including the TMD of Vpu, Vpu1–32, and Vpu8–26, are presented by using a combination of classical molecular dynamics (MD) simulations combined with a docking approach. The rim of alanines (Ala‐8, ‐11, ‐15, and ‐19) resembles an interlocking motif for the sequential assembly into a dimer and trimer. Simultaneous assembly results in oligomeric bundles (trimers to pentamers) with either tryptophans (Trp‐23) or purely hydrophobic residues facing the center. Bundles, with serines facing the pore (Ser‐24), are energetically not the lowest structures. For pentameric bundles with Ser‐24 facing the pore, no water column develops during a short 25 ns MD simulation. © 2013 Wiley Periodicals, Inc. Biopolymers 99: 517–529, 2013.</div>
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Assembling viral channel forming proteins: Vpu from HIV‐1

Assembling viral channel forming proteins: Vpu from HIV‐1

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri