A substrate-driven allosteric switch that enhances PDI catalytic activity

Autor: Roelof H. Bekendam, Pavan K. Bendapudi, Lin Lin, Partha P. Nag, Jun Pu, Daniel R. Kennedy, Alexandra Feldenzer, Joyce Chiu, Kristina M. Cook, Bruce Furie, Mingdong Huang, Philip J. Hogg, Robert Flaumenhaft
Jazyk: angličtina
Rok vydání: 2016
Předmět:
Zdroj: Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/ncomms12579
Popis: Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational change in the catalytic domains and inhibiting thrombosis.
Databáze: Directory of Open Access Journals