Interaction analysis of buffalo pregnancy associated glycoprotein-1 in silico

Abstract

Pregnancy associated glycoprotein-1, a member of the aspartic proteinase family possesses placentogenic and embryo protective functions in numerous domestic species. The present study was conducted to deduce binding and interaction properties of buffalo pregnancy associated glycoprotein-1 (PAG-1) in silico. Buffalo PAG-1 DNA, RNA binding sites deduced using BindN server revealed buffalo PAG-1 protein sequence possess 93 residues with 80% and 56.96% DNA binding specificity and sensitivity, respectively. RNA binding sites are also restricted to identical clusters of amino acid residues as DNA binding sites with 78 residues with RNA binding potential with 80% specificity and 53.95% sensitivity. The potential domains with a high degree of DNA and RNA binding property are present at conserved microsequences residues of buffalo PAG-1 protein sequence. Ligand binding properties from PDBSUM database reveal buffalo PAG-1 possesses ten clefts having potential ligand binding sites consisting of aliphatic and positive amino acid residues. Analysis with the STRING database showed buffalo PAG-1 interaction with cytokines viz. phosphoprotein associated with glycosphingolipid microdomains 1, placenta growth factor precursor, alpha-fetoprotein precursor and SP1 transcription factor. These factors are found to be active during the embryonic stage exerting their functions through angiogenesis, endothelial cell growth, proliferation, migration and differentiation. In conclusion this study reports the various binding properties and putative functional interactions of buffalo pregnancy associated glycoprotein-1 with other cytokines for exerting its biological action.