Figure 1.
FVIII is constitutively produced as multiple partially disulfide-bonded states. (A) Ribbon representation of the AlphaFold structure of human VIII lacking the unstructured B domain that does not contain disulfide bonds. The domains (A1, A2, A3, C1, and C2) are color coded, and the 8 disulfide bonds are shown as yellow spheres and residue numbers indicated (UniProt P00451 numbering). (B) Incidence of unformed disulfide bonds in human plasma FVIII (n = 3 preparations of cryoprecipitated plasma, Factane) and (C) recombinant FVIII (n = 3 FVIII preparations). For example, the A3 domain C1918-C1922 bond is unformed in ∼70% (plasma) or ∼50% (recombinant) of molecules of the FVIII samples. The C2193-C2345 disulfide cysteines were not able to be resolved in the plasma sample. The bars and errors are mean ± standard deviation (SD).

FVIII is constitutively produced as multiple partially disulfide-bonded states. (A) Ribbon representation of the AlphaFold structure of human VIII lacking the unstructured B domain that does not contain disulfide bonds. The domains (A1, A2, A3, C1, and C2) are color coded, and the 8 disulfide bonds are shown as yellow spheres and residue numbers indicated (UniProt P00451 numbering). (B) Incidence of unformed disulfide bonds in human plasma FVIII (n = 3 preparations of cryoprecipitated plasma, Factane) and (C) recombinant FVIII (n = 3 FVIII preparations). For example, the A3 domain C1918-C1922 bond is unformed in ∼70% (plasma) or ∼50% (recombinant) of molecules of the FVIII samples. The C2193-C2345 disulfide cysteines were not able to be resolved in the plasma sample. The bars and errors are mean ± standard deviation (SD).

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal