Protein M2-1 forms tetramers

Stable Identifier
R-HSA-9830270
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Protein M2-1 forms tetramers
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Protein M2-1, one of the two protein products of the M2 gene of human respiratory syncytial virus (hRSV) that acts as an antiterminator/processivity factor for the RSV RNA-dependent RNA polymerase (RdRP), forms disk-like tetramers. Tetramer formation requires one zinc ion per M2-1 monomer for stability (Tran et al, 2009; Tanner et al, 2014; Molina et al, 2018; Gao et al, 2020; Esperante et al. 2012).
Literature References
PubMed ID Title Journal Year
19386701 The respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner

Tran, TL, Castagné, N, Dubosclard, V, Noinville, S, Koch, E, Moudjou, M, Henry, C, Bernard, J, Yeo, RP, Eléouët, JF

J Virol 2009
24434552 Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation

Tanner, SJ, Ariza, A, Richard, CA, Kyle, HF, Dods, RL, Blondot, ML, Wu, W, Trincão, J, Trinh, CH, Hiscox, JA, Carroll, MW, Silman, NJ, Eléouët, JF, Edwards, TA, Barr, JN

Proc Natl Acad Sci U S A 2014
32697936 Structure of the Human Respiratory Syncytial Virus M2-1 Protein in Complex with a Short Positive-Sense Gene-End RNA

Gao, Y, Cao, D, Pawnikar, S, John, KP, Ahn, HM, Hill, S, Ha, JM, Parikh, P, Ogilvie, C, Swain, A, Yang, A, Bell, A, Salazar, A, Miao, Y, Liang, B

Structure 2020
29372904 Structure and stability of the Human respiratory syncytial virus M2-1 RNA-binding core domain reveals a compact and cooperative folding unit

Molina, IG, Josts, I, Almeida Hernandez, Y, Esperante, S, Salgueiro, M, Garcia Alai, MM, de Prat-Gay, G, Tidow, H

Acta Crystallogr F Struct Biol Commun 2018
22978633 Modular unfolding and dissociation of the human respiratory syncytial virus phosphoprotein p and its interaction with the m(2-1) antiterminator: a singular tetramer-tetramer interface arrangement

Esperante, SA, Paris, G, de Prat-Gay, G

Biochemistry 2012
Participants
Input
Output
Participates
as an event of
Disease
Cross References
Mondo
Authored
Stephan, R  (2023-03-24)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Orlic-Milacic, M  (2023-03-02)
Cite Us!