[HTML][HTML] Allosteric disulfide bonds in thrombosis and thrombolysis

VM Chen, PJ Hogg - Journal of Thrombosis and Haemostasis, 2006 - Elsevier
Allosteric disulfide bonds control protein function by mediating conformational change when
they undergo reduction or oxidation. The known allosteric disulfide bonds are characterized
by a particular bond geometry, the− RHStaple. A number of thrombosis and thrombolysis
proteins contain one or more disulfide bonds of this type. Tissue factor (TF) was the first
hemostasis protein shown to be controlled by an allosteric disulfide bond, the Cys186–
Cys209 bond in the membrane‐proximal fibronectin type III domain. TF exists in three forms …