= J. A. Huntington
{c}
<J. A. Huntington> is the first author of a 2000 structural study explaining how an inhibitory <serpin> can trap and deform a <protease>. The team determined a <crystal structure> of the joined <serpin>–<protease> complex, connecting a large conformational change to loss of catalytic function.<Structure of a serpin-protease complex shows inhibition by deformation by J. A. Huntington and others>[Original byline and Abstract]{ref}
Attack on the <reactive-center loop> was associated with movement of the tethered region about $71\,\mathrm{\mathring A}$ across the <serpin>. The attached <protease> was distorted, including disruption of its <active site>.<Structure of a serpin-protease complex shows inhibition by deformation by J. A. Huntington and others>[Abstract: displacement and protease deformation]{ref}
This gives a physical explanation for inhibition beyond simple obstruction of an <active site>. The <protein> scaffold changes shape after attack and carries the reacting partner into an unfavourable arrangement. The structural result identifies the trapped arrangement; the detailed time course of the moving complex remains a separate experimental question.
Back to article page
