Understanding the effect of residue mutations on collagen structure and interactions
Collagen, the most abundant protein in the extracellular matrix (ECM), provides physical support for cells and organs. Collagen also plays central and dynamic roles in ECM remodeling, cell migration and adhesion, and mediates other important biological processes via its interactions with a diverse array of binding partners. A molecular level comprehension of how these factors impact collagen structure and interactions is important not just from a fundamental perspective, but also because mutations in collagen are implicated in various diseases, including osteogenesis imperfecta, Ehlers-Danlos syndrome, and Alport syndrome. Our group is using molecular dynamics simulations to provide insights into how mutations affect the characteristic triple helical structure of collagen and its interaction with other proteins.