4ju5 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 A 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.
Structural insight into the dimerization of human protein disulfide isomerase.,Bastos-Aristizabal S, Kozlov G, Gehring K Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Bastos-Aristizabal S, Kozlov G, Gehring K. Structural insight into the dimerization of human protein disulfide isomerase. Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644 doi:http://dx.doi.org/10.1002/pro.2444
