„Dinosaur Collagen‟ Computational Structure Modelling and Docking Analysis with α1 (I) Integrin Domain

Three peptides from two unique collagen sequences (α1 and α2 chains) of two dinosaur species i.e. Tyrannosaurus rex and Brachylophosaurus canadensis had previously been found to overlap with the integrin binding site on the rat collagen microfibril structure and was reported to be a significant non-random distribution suggesting mechanisms of protein survival over long geologic periods. The sequences of these peptides featuring certain conserved residues as was revealed by analyzing multiple alignments from different organisms, functional importance of recognition motif and the nature of collagen itself favoring conservation, were used to computationally model the triple helix structure and the resultant structure was docked with the crystal structure of α1 (I) Integrin domain (PDB Code-2M32). Similar patterns of interaction were observed between the receptor i.e. α1 (I) Integrin domain and each of the different ligands i.e. modelled collagen structure of the two dinosaur species and the synthetic collagen mimetic peptide (present in the original complex of 2M32).