Download MendeleyHigh-resolution crystal structures of factor XIa coagulation factor in complex with nonbasic high-affinity synthetic inhibitors.
Fradera, X., Kazemier, B., Carswell, E., Cooke, A., Oubrie, A., Hamilton, W., Dempster, M., Krapp, S., Nagel, S., Jestel, A.(2012) Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 404-408
- PubMed: 22505407
- DOI: https://doi.org/10.1107/S1744309112009037
- Primary Citation of Related Structures:
3SOR, 3SOS - PubMed Abstract:
Factor XI (FXI) is a key enzyme in the coagulation pathway and an attractive target for the development of anticoagulant drugs. A small number of high-resolution crystal structures of FXIa in complex with small synthetic inhibitors have been published to date. All of these ligands have a basic P1 group and bind exclusively in the nonprime side of the active site of FXIa. Here, two structures of FXIa in complex with nonbasic inhibitors that occupy both the prime and nonprime sides of the active site are presented. These new structures could be valuable in the design and optimization of new FXIa synthethic inhibitors.
Organizational Affiliation:
Merck Research Laboratories, MSD, Newhouse, Lanarkshire ML1 5SH, Scotland. [email protected]
