Author(s): Ganguly Bhaskar | Prasad Shiv
Journal: Journal of Animal Science and Biotechnology
ISSN 1674-9782
Volume: 3;
Issue: 1;
Start page: 13;
Date: 2012;
Original page
Keywords: Bubaline | Homology modeling | Pregnancy associated glycoprotein (PAG) | Structure | Function
ABSTRACT
Abstract Background Pregnancy associated glycoproteins form a diverse family of glycoproteins that are variably expressed at different stages of gestation. They are probably involved in immunosuppression of the dam against the feto-maternal placentome. The presence of the products of binucleate cells in maternal circulation has also been correlated with placentogenesis and placental re-modeling. The exact structure and function of the gene product is unknown due to limitations on obtaining purified pregnancy associated glycoprotein preparations. Results Our study describes an in silico derived 3D model for bubaline pregnancy associated glycoprotein 2. Structure-activity features of the protein were characterized, and functional studies predict bubaline pregnancy associated glycoprotein 2 as an inducible, extra-cellular, non-essential, N-glycosylated, aspartic pro-endopeptidase that is involved in down-regulation of complement pathway and immunity during pregnancy. The protein is also predicted to be involved in nutritional processes, and apoptotic processes underlying fetal morphogenesis and re-modeling of feto-maternal tissues. Conclusion The structural and functional annotation of buPAG2 shall allow the designing of mutants and inhibitors for dissection of the exact physiological role of the protein.
Journal: Journal of Animal Science and Biotechnology
ISSN 1674-9782
Volume: 3;
Issue: 1;
Start page: 13;
Date: 2012;
Original page
Keywords: Bubaline | Homology modeling | Pregnancy associated glycoprotein (PAG) | Structure | Function
ABSTRACT
Abstract Background Pregnancy associated glycoproteins form a diverse family of glycoproteins that are variably expressed at different stages of gestation. They are probably involved in immunosuppression of the dam against the feto-maternal placentome. The presence of the products of binucleate cells in maternal circulation has also been correlated with placentogenesis and placental re-modeling. The exact structure and function of the gene product is unknown due to limitations on obtaining purified pregnancy associated glycoprotein preparations. Results Our study describes an in silico derived 3D model for bubaline pregnancy associated glycoprotein 2. Structure-activity features of the protein were characterized, and functional studies predict bubaline pregnancy associated glycoprotein 2 as an inducible, extra-cellular, non-essential, N-glycosylated, aspartic pro-endopeptidase that is involved in down-regulation of complement pathway and immunity during pregnancy. The protein is also predicted to be involved in nutritional processes, and apoptotic processes underlying fetal morphogenesis and re-modeling of feto-maternal tissues. Conclusion The structural and functional annotation of buPAG2 shall allow the designing of mutants and inhibitors for dissection of the exact physiological role of the protein.
