University of Oulu

Nguyen, V., Biterova, E., Salin, M., Wierenga, R., Ruddock, L. (2018) Crystal structure of human anterior gradient protein 3. Acta Crystallographica Section F: Structural Biology Communications, 74 (7), 425-430. doi:10.1107/S2053230X18009093

Crystal structure of human anterior gradient protein 3

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Author: Nguyen, V. D.1; Biterova, E.1; Salin, M.1;
Organizations: 1Faculty of Biochemistry and Molecular Medicine, University of Oulu
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 0.6 MB)
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Language: English
Published: John Wiley & Sons, 2018
Publish Date: 2019-02-21


Oxidative protein folding in the endoplasmic reticulum is catalyzed by the protein disulfide isomerase family of proteins. Of the 20 recognized human family members, the structures of eight have been deposited in the PDB along with domains from six more. Three members of this family, ERp18, anterior gradient protein 2 (AGR2) and anterior gradient protein 3 (AGR3), are single-domain proteins which share sequence similarity. While ERp18 has a canonical active-site motif and is involved in native disulfide-bond formation, AGR2 and AGR3 lack elements of the active-site motif found in other family members and may both interact with mucins. In order to better define its function, the structure of AGR3 is required. Here, the recombinant expression, purification, crystallization and crystal structure of human AGR3 are described.

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Series: Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
ISSN-E: 2053-230X
ISSN-L: 2053-230X
Volume: 74
Issue: 7
Pages: 425 - 430
DOI: 10.1107/S2053230X18009093
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: Funding for this research was provided by: Academy of Finland, Biotieteiden ja Ympäristön Tutkimuksen Toimikunta; Sigrid Juséliuksen Säätiö; Biocenter Oulu.
Dataset Reference: 3D view
PDB reference: human anterior gradient protein 3, 3ph9
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