Structural basis of transcobalamin recognition by human CD320 receptor

Amer Alam; Jae-Sung Woo; Jennifer Schmitz; Bernadette Prinz; Katharina Root; Fan Chen; Joël S. Bloch; Renato Zenobi; Kaspar P. Locher

doi:10.1038/ncomms12100

Nature Communications (Jul 2016)

Structural basis of transcobalamin recognition by human CD320 receptor

Amer Alam,
Jae-Sung Woo,
Jennifer Schmitz,
Bernadette Prinz,
Katharina Root,
Fan Chen,
Joël S. Bloch,
Renato Zenobi,
Kaspar P. Locher

Affiliations

Amer Alam: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich
Jae-Sung Woo: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich
Jennifer Schmitz: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich
Bernadette Prinz: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich
Katharina Root: Department of Chemistry and Applied Biosciences, ETH Zurich
Fan Chen: Department of Chemistry and Applied Biosciences, ETH Zurich
Joël S. Bloch: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich
Renato Zenobi: Department of Chemistry and Applied Biosciences, ETH Zurich
Kaspar P. Locher: Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich

DOI: https://doi.org/10.1038/ncomms12100
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 9

Abstract

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Cellular uptake of vitamin B12 (cobalamin) requires the binding of holo-transcobalamin (TC) from plasma by CD320. Here, the authors report the structure of a complex between CD320 and TC loaded with cyanocobalamin, alongside additional functional analysis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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