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• W2101356043 endingPage "2541" @default.
• W2101356043 startingPage "2533" @default.
• W2101356043 abstract "SummaryAllosteric 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 on the cell surface: a cryptic form that is inert, a coagulant form that rapidly binds factor VIIa to initiate coagulation, and a signaling form that binds FVIIa and cleaves protease‐activated receptor 2, which functions in inflammation, tumor progression and angiogenesis. Reduction and oxidation of the Cys186–Cys209 disulfide bond is central to the transition between the three forms of TF. The redox state of the bond appears to be controlled by protein disulfide isomerase and NO. Plasmin(ogen), vitronectin, glycoprotein 1bα, integrin β3 and thrombomodulin also contain −RHStaple disulfides, and there is circumstantial evidence that the function of these proteins may involve cleavage/formation of these disulfide bonds. 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 on the cell surface: a cryptic form that is inert, a coagulant form that rapidly binds factor VIIa to initiate coagulation, and a signaling form that binds FVIIa and cleaves protease‐activated receptor 2, which functions in inflammation, tumor progression and angiogenesis. Reduction and oxidation of the Cys186–Cys209 disulfide bond is central to the transition between the three forms of TF. The redox state of the bond appears to be controlled by protein disulfide isomerase and NO. Plasmin(ogen), vitronectin, glycoprotein 1bα, integrin β3 and thrombomodulin also contain −RHStaple disulfides, and there is circumstantial evidence that the function of these proteins may involve cleavage/formation of these disulfide bonds." @default.
• W2101356043 created "2016-06-24" @default.
• W2101356043 creator A5008060768 @default.
• W2101356043 creator A5030789412 @default.
• W2101356043 date "2006-12-01" @default.
• W2101356043 modified "2023-10-13" @default.
• W2101356043 title "Allosteric disulfide bonds in thrombosis and thrombolysis" @default.
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• W2101356043 doi "https://doi.org/10.1111/j.1538-7836.2006.02236.x" @default.
• W2101356043 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17002656" @default.
• W2101356043 hasPublicationYear "2006" @default.
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