F1 binds to F2 forming the F subunit

Stable Identifier
R-HSA-9829183
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
trans-Golgi network membrane
ReviewStatus
5/5
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F1 binds to F2 forming the F subunit
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F1 and F2 proteins of respiratory syncytial virus (RSV) interact forming a disulfide-linked dimer. Interchain disulfide bonds located at Cys37-Cys439 and Cys69-Cys212 have been shown in crystal structures of the trimeric F ectodomain in its postfusion conformation (Walsh et al, 1985; Arumugham et al, 1989; Day et al, 2006; McLellan et al, 2011).
Literature References
PubMed ID Title Journal Year
16723026 Contribution of cysteine residues in the extracellular domain of the F protein of human respiratory syncytial virus to its function

Day, ND, Branigan, PJ, Gutshall, LL, Liu, C, Sarisky, RT, Melero, JA, Del Vecchio, AM, Luo, J

Virol J 2006
3838336 Purification and characterization of the respiratory syncytial virus fusion protein

Walsh, EE, Schlesinger, JJ, Brandriss, MW

J Gen Virol 1985
21613394 Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes

Kwong, PD, Graham, BS, McLellan, JS, Yang, Y

J Virol 2011
2774976 Evidence that the fusion protein of respiratory syncytial virus exists as a dimer in its native form. Brief report

Arumugham, RG, Paradiso, PR, Hildreth, SW

Arch Virol 1989
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Authored
Stephan, R  (2023-02-22)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-02-24)
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