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Ganguly B, Prasad S. Homology modeling and functional annotation of bubaline pregnancy associated glycoprotein 2. J Anim Sci Biotechnol. 2012;3(1):13doi: 10.1186/2049-1891-3-13.
Ganguly, B., & Prasad, S. (2012). Homology modeling and functional annotation of bubaline pregnancy associated glycoprotein 2. Journal of animal science and biotechnology, 3(1), 13. https://doi.org/10.1186/2049-1891-3-13
Ganguly, Bhaskar, and Prasad, Shiv. "Homology modeling and functional annotation of bubaline pregnancy associated glycoprotein 2." Journal of animal science and biotechnology vol. 3,1 (2012): 13. doi: https://doi.org/10.1186/2049-1891-3-13
Ganguly B, Prasad S. Homology modeling and functional annotation of bubaline pregnancy associated glycoprotein 2. J Anim Sci Biotechnol. 2012 May 31;3(1):13. doi: 10.1186/2049-1891-3-13. PMID: 22958467; PMCID: PMC3436636.
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J Anim Sci Biotechnol. 2012 May 31;3(1):13. doi: 10.1186/2049-1891-3-13.

Homology modeling and functional annotation of bubaline pregnancy associated glycoprotein 2.

Journal of animal science and biotechnology

Bhaskar Ganguly, Shiv Prasad

Affiliations

  1. Department of Veterinary Physiology and Biochemistry, College of Veterinary and Animal Sciences, G, B, Pant University of Agriculture and Technology, Pantnagar, PIN: 263145, India. [email protected].

PMID: 22958467 PMCID: PMC3436636 DOI: 10.1186/2049-1891-3-13

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.

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