4JU5

Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase

Summary for 4JU5

Entry DOI	10.2210/pdb4ju5/pdb
Descriptor	Protein disulfide-isomerase (2 entities in total)
Functional Keywords	thioredoxin-like fold, disulfide isomerase, chaperone, isomerase
Biological source	Homo sapiens (human)
Total number of polymer chains	2
Total formula weight	53670.51
Authors	Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K. (deposition date: 2013-03-24, release date: 2014-02-19, Last modification date: 2023-09-20)
Primary citation	Bastos-Aristizabal, S.,Kozlov, G.,Gehring, K. Structural insight into the dimerization of human protein disulfide isomerase. Protein Sci., 23:618-626, 2014 Cited by PubMed Abstract: Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). Here, it is shown that human PDI (PDIA1) dimerizes in vivo and proposed that the dimerization of PDI has physiological relevance by autoregulating its activity. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 Å resolution revealed that the formation of dimers occludes the substrate binding site and may function as a mechanism to regulate PDI activity in the ER. PubMed: 24549644 DOI: 10.1002/pro.2444 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.28 Å)

Structure validation