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 4
Small-angle X-ray scattering (SAXS) analysis of the M_2–1 RBD. (a) Raw scattering profile of the HRSV M_2–1 RBD with the Guinier region shown in the inset. (b) Kratky plot suggesting the presence of a folded core with a flexible tail. (c) Distance distribution plot. (d) Ab initio shape reconstruction (grey) superimposed on the crystal structure of the HRSV M_2–1 RBD (PDB entry 5noh; blue). The N- and C-termini of the protein are highlighted in green and red, respectively.

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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