James A. Huntington

TL;DR: A new structure analyzed in context of other recent structures and biochemical studies emerges that involves a change in the mode of binding of the F2 domain (fragment 2) on the catalytic domain after cleavage at Arg320, and a subsequent reorientation of the linker between the F1 and catalyticdomain to present the Arg271 site for cleavage.

TL;DR: Small-angle x-ray scattering was used to characterize Z- α1AT polymers in solution and showed that the Z-α1AT trimer, tetramer, and pentamer all form ring-like structures in strong support of a common domain-swap polymerization mechanism that can lead to self-terminating polymers.

TL;DR: The crystal structure of Pseutarin C is used as a starting point for homology modelling and assembly of the full human prothrombinase complex and provides a powerful resource for contextualizing previous data and for designing future experiments.

TL;DR: It is concluded that an inescapable consequence of the loop-sheet mechanism is polymer compaction and rigidity, properties that are inconsistent with the ‘beads-on-a-string’ morphology of polymers obtained from human tissue.

TL;DR: Iripin-8, a salivary serpin from the tick Ixodes ricinus, a European vector of tick-borne encephalitis and Lyme disease, was characterized in this article.