Unknown

Dataset Information

0

Crystal structure of human anterior gradient protein 3.


ABSTRACT: 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.

SUBMITTER: Nguyen VD 

PROVIDER: S-EPMC6038452 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of human anterior gradient protein 3.

Nguyen Van Dat VD   Biterova Ekaterina E   Salin Mikko M   Wierenga Rik K RK   Ruddock Lloyd W LW  

Acta crystallographica. Section F, Structural biology communications 20180626 Pt 7


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 d  ...[more]

Similar Datasets

| S-EPMC4839744 | biostudies-literature
| S-EPMC4039089 | biostudies-literature
| S-EPMC5044835 | biostudies-literature
| S-EPMC4859480 | biostudies-literature
| S-EPMC6717300 | biostudies-literature
| S-EPMC2286586 | biostudies-literature
| S-EPMC5563145 | biostudies-literature
| S-EPMC2637903 | biostudies-literature
| S-EPMC10868460 | biostudies-literature
| S-EPMC5287372 | biostudies-literature