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This study aimed to perform in silico analyses of the primary and secondary structures of the bovine chemokine receptor CXCR1, the non-polymorphic and A122V-harboring polymorphic proteins to predict differences. Two sequences of the CXCR1 protein of Bos taurus cattle were selected from the non-redundant protein sequence database UniProtKB/Swiss-Prot: a) a non-polymorphic sequence (A7KWG0), with alanine (A) at position 122, and b) a sequence harboring the causal polymorphism A122V with substitution by valine (V) at the same position. Protein primary and secondary structures were analyzed using the ProtParam program and Chou & Fasman Protein Secondary Structure Prediction CFSSP algorithm. No differences in physical or chemical parameters were predicted from the primary structure of the two bovine protein sequences. The presence of a helix domain situated between positions 100 and 150 was only found in the non-polymorphic CXCR1 protein. Amino acid residues with different biochemical features were detected at position 122 in the ruminant and human CXCR1 protein sequences, suggesting that this peptide seems to be highly polymorphic in vertebrates. Findings described herein predict differences in the secondary structure pattern of non-polymorphic and polymorphic A122V-harboring CXCR1 proteins using bioinformatics tools

biotemas

Predicting the effects of the single nucleotide polymorphism A122V on CXC chemokine receptor type 1 of Bos taurus (Artiodactyla: Bovidae) cattle by in silico analyses