All Outputs (4)

Crystal structure and substrate-induced activation of ADAMTS13 (2019)
Journal Article
Petri, A., Kim, H. J., Xu, Y., de Groot, R., Li, C., Vandenbulcke, A., Vanhoorelbeke, K., Emsley, J., & Crawley, J. T. (2019). Crystal structure and substrate-induced activation of ADAMTS13. Nature Communications, 10, Article 3781. https://doi.org/10.1038/s41467-019-11474-5

Platelet recruitment to sites of blood vessel damage is highly dependent upon von Willebrand factor (VWF). VWF platelet-tethering function is proteolytically regulated by the metalloprotease ADAMTS13. Proteolysis depends upon shear-induced conformati... Read More about Crystal structure and substrate-induced activation of ADAMTS13.

Crystal structures of the recombinant β-factor XIIa protease with bound Thr-Arg and Pro-Arg substrate mimetics (2019)
Journal Article
Pathak, M., Manna, R., Li, C., Kaira, B. G., Hamad, B. K., Belviso, B. D., Bonturi, C. R., Dreveny, I., Fischer, P. M., Dekker, L. V., Oliva, M. L. V., & Emsley, J. (2019). Crystal structures of the recombinant β-factor XIIa protease with bound Thr-Arg and Pro-Arg substrate mimetics. Acta Crystallographica. Section d, Structural Biology, 75(6), 578-591. https://doi.org/10.1107/s2059798319006910

© 2019 International Union of Crystallography. Coagulation factor XII (FXII) is a key initiator of the contact pathway, which contributes to inflammatory pathways. FXII circulates as a zymogen, which when auto-activated forms factor XIIa (FXIIa). Her... Read More about Crystal structures of the recombinant β-factor XIIa protease with bound Thr-Arg and Pro-Arg substrate mimetics.

Structural basis of the leukocyte integrin Mac-1 I-domain interactions with the platelet glycoprotein Ib (2019)
Journal Article
Morgan, J., Saleem, M., Ng, R., Armstrong, C., Wong, S. S., Caulton, S. G., Fickling, A., Williams, H. E., Munday, A. D., Lopez, J. A., Searle, M. S., & Emsley, J. (2019). Structural basis of the leukocyte integrin Mac-1 I-domain interactions with the platelet glycoprotein Ib. Blood Advances, 3(9), 1450-1459. https://doi.org/10.1182/bloodadvances.2018027011

Cell-surface receptor interactions between leukocyte integrin macrophage-1 antigen (Mac-1, also known as CR3, aMb2, CD11b/CD18) and platelet glycoprotein Iba (GPIba) are critical to vascular inflammation. To define the key residues at the binding inter... Read More about Structural basis of the leukocyte integrin Mac-1 I-domain interactions with the platelet glycoprotein Ib.

Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI (2019)
Journal Article
Li, C., Voos, K. M., Pathak, M., Hall, G., McCrae, K. R., Dreveny, I., Li, R., & Emsley, J. (2019). Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI. Journal of Thrombosis and Haemostasis, 17(5), 759-770. https://doi.org/10.1111/jth.14418

Background
Plasma prekallikrein (PK) and factor XI (FXI) are apple domain‐containing serine proteases that when activated to PKa and FXIa cleave substrates kininogen, factor XII, and factor IX, respectively, directing plasma coagulation, bradykinin... Read More about Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI.