Antithrombin, the main inhibitor of thrombosis in blood, is bound and
activated by the heparin-like side-chains that line the small vasculat
ure. We now have good depictions of the heparin-binding site on antith
rombin, and of the way in which mutations at this site cause thromboti
c disease. The interaction of heparin with antithrombin is, however, a
kinetic one, with binding being followed by formation of a complex wi
th thrombin and then release from the heparin. Our understanding of th
e processes involved is currently based on crystallographic models but
, for a mobile mechanism, these merely provide snapshots - what is nee
ded is a movie.