Sikora, Jacqueline. Towards determining the mechanism of recognition and binding to collagen by alpha 1 beta 1 and alpha 2 beta 1 integrins. Retrieved from https://doi.org/doi:10.7282/T36Q1ZVC
DescriptionCollagen is the most abundant protein in the human body. There are several collagen‐binding integrins, which exist as transmembrane proteins and serve to transmit cellular signals via inside‐out and outside‐in pathways, via a cascade of conformational changes. Collagen is capable of initiating outside‐in signaling by binding to the extracellular I‐domain of integrin, in a cation‐dependent manner. While much is known about collagen subtype and sequence specificity of varying integrins, the mechanism of binding has yet to be determined. Our lab studies the interaction between collagen and the I‐domains of integrins alpha 1 beta 1 (alpha1I), and alpha 2 beta 1 (alpha2I), via molecular biology and nuclear magnetic resonance (NMR) techniques. We are also investigating recombinant collagen‐like peptides for the purpose of binding assays between collagen and integrin. The goal is to determine a structuralfunctional relationship occurring in the interaction, and to use this in order to determine the mechanism of binding. The interaction of collagen and integrin has roles in cancer cell proliferation and thrombosis, making the determination of this mechanism vital to the generation of future treatments for these diseases.