Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography

Liya Hu; Wilhelm Salmen; Banumathi Sankaran; Yi Lasanajak; David F. Smith; Sue E. Crawford; Mary K. Estes; B. V. Venkataram Prasad

doi:10.1038/s42003-022-03357-1

Communications Biology (May 2022)

Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography

Liya Hu,
Wilhelm Salmen,
Banumathi Sankaran,
Yi Lasanajak,
David F. Smith,
Sue E. Crawford,
Mary K. Estes,
B. V. Venkataram Prasad

Affiliations

Liya Hu: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine
Wilhelm Salmen: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine
Banumathi Sankaran: Berkeley Center for Structural Biology, Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley Laboratory
Yi Lasanajak: Emory Glycomics and Molecular Interactions Core (EGMIC), Emory University School of Medicine
David F. Smith: Emory Glycomics and Molecular Interactions Core (EGMIC), Emory University School of Medicine
Sue E. Crawford: Department of Molecular Virology and Microbiology, Baylor College of Medicine
Mary K. Estes: Department of Molecular Virology and Microbiology, Baylor College of Medicine
B. V. Venkataram Prasad: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine

DOI: https://doi.org/10.1038/s42003-022-03357-1
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 8

Abstract

Read online

Group B rotaviruses have a unique fold in the glycan-binding domain specific for N- acetyllactosamine that potentially diverged from folds conserved in group A and C rotaviruses.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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