SH forms a pentamer

Stable Identifier
R-HSA-9831126
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
trans-Golgi network membrane
ReviewStatus
5/5
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SH forms a pentamer
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In membranes, SH forms a homopentameric ion channel that acts as a viroporin, inducing membrane permeability and selective transport of sodium and potassium ions (Gan et al, 2008; Carter et al, 2010; Gan et al, 2012; Li et al, 2014; Araujo et al, 2016).
Literature References
PubMed ID Title Journal Year
25100835 Inhibition of the human respiratory syncytial virus small hydrophobic protein and structural variations in a bicelle environment

Li, Y, To, J, Verdiá-Báguena, C, Dossena, S, Surya, W, Huang, M, Paulmichl, M, Liu, DX, Aguilella, VM, Torres, J

J Virol 2014
27817112 Structure and functional dynamics characterization of the ion channel of the human respiratory syncytial virus (hRSV) small hydrophobic protein (SH) transmembrane domain by combining molecular dynamics with excited normal modes

Araujo, GC, Silva, RH, Scott, LP, Araujo, AS, Souza, FP, de Oliveira, RJ

J Mol Model 2016
20471980 Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability

Carter, SD, Dent, KC, Atkins, E, Foster, TL, Verow, M, Gorny, P, Harris, M, Hiscox, JA, Ranson, NA, Griffin, S, Barr, JN

FEBS Lett 2010
22621926 The small hydrophobic protein of the human respiratory syncytial virus forms pentameric ion channels

Gan, SW, Tan, E, Lin, X, Yu, D, Wang, J, Tan, GM, Vararattanavech, A, Yeo, CY, Soon, CH, Soong, TW, Pervushin, K, Torres, J

J Biol Chem 2012
18369195 Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain

Gan, SW, Ng, L, Lin, X, Gong, X, Torres, J

Protein Sci 2008
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Disease
Cross References
Mondo
Authored
Stephan, R  (2023-03-16)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-03-19)
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