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Crystal structure of human anterior gradient protein 3
Author(s) -
Nguyen Van Dat,
Biterova Ekaterina,
Salin Mikko,
Wierenga Rik K.,
Ruddock Lloyd W.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18009093
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , protein folding , chaperone (clinical) , protein data bank (rcsb pdb) , biochemistry , chemistry , recombinant dna , protein structure , biology , microbiology and biotechnology , gene , medicine , pathology
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.