Yu-Shan Lin
Tufts Chemistry


Home

↘ Research

↘ People

Papers

Outreach

News

↘ Contact

Yu-Shan Lin
Department of Chemistry
Tufts University
62 Talbot Avenue Pearson 103-X
Medford, MA 02155

Email: yu-shan.lin@tufts.edu

Collagen

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.

P. Chhum, H. Yu, B. An, B. Doyon, Y.-S. Lin,* B. Brodsky,* “Consequences of glycine mutations in the fibronectin binding sequence of collagen,” J. Biol. Chem. 291, 27073‒27086 (2016).
Equal contributions. *Co-corresponding authors.

S. Yigit, H. Yu, B. An, S. Hamaia, R. W. Farndale, D. L. Kaplan, Y.-S. Lin,* B. Brodsky,* “Mapping the effect of Gly mutations in collagen on α2β1 integrin binding,” J. Biol. Chem. 291, 19196‒19207 (2016).
Equal contributions. *Co-corresponding authors.

B. An, Y.-S. Lin, B. Brodsky, “Collagen interactions: Drug design and delivery,” Adv. Drug Deliv. Rev. 97, 69‒82 (2016).