Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum

Valeriu Bortnov; Marco Tonelli; Woonghee Lee; Ziqing Lin; Douglas S. Annis; Omar N. Demerdash; Alex Bateman; Julie C. Mitchell; Ying Ge; John L. Markley; Deane F. Mosher

doi:10.1038/s41467-019-13577-5

Nature Communications (Dec 2019)

Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum

Valeriu Bortnov,
Marco Tonelli,
Woonghee Lee,
Ziqing Lin,
Douglas S. Annis,
Omar N. Demerdash,
Alex Bateman,
Julie C. Mitchell,
Ying Ge,
John L. Markley,
Deane F. Mosher

Affiliations

Valeriu Bortnov: Department of Biomolecular Chemistry, University of Wisconsin-Madison
Marco Tonelli: Department of Biochemistry, University of Wisconsin-Madison
Woonghee Lee: Department of Biochemistry, University of Wisconsin-Madison
Ziqing Lin: Departments of Cell and Regenerative Biology and Chemistry, University of Wisconsin-Madison
Douglas S. Annis: Department of Biomolecular Chemistry, University of Wisconsin-Madison
Omar N. Demerdash: Biosciences Division, Oak Ridge National Laboratory
Alex Bateman: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus
Julie C. Mitchell: Biosciences Division, Oak Ridge National Laboratory
Ying Ge: Departments of Cell and Regenerative Biology and Chemistry, University of Wisconsin-Madison
John L. Markley: Department of Biochemistry, University of Wisconsin-Madison
Deane F. Mosher: Department of Biomolecular Chemistry, University of Wisconsin-Madison

DOI: https://doi.org/10.1038/s41467-019-13577-5
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 14

Abstract

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Myeloid-derived growth factor (MYDGF) is an endoplasmic reticulum protein of therapeutic interest because it promotes tissue repair in a murine model of myocardial infarction. Here the authors present the NMR structure of human MYDGF and attribute function to a set of residues conserved in MYDGFs but not the vanin base domain, which has a similar fold.

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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