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

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

doi:10.1107/S2053230X17017381

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Domain interactions in tetrameric full-length HRSV M_2–1. One monomer within the tetrameric full-length protein is coloured; the other three monomers are displayed in grey tones. The tetramerization domain is coloured yellow, the zinc-binding domain is in orange, the Zn²⁺ ion is in magenta and the RBD core domain is in cyan (PDB entry 4c3b).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 74| Part 1| January 2018| Pages 23-30

https://doi.org/10.1107/S2053230X17017381

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