The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion

Table 1 Mutations of disulfide bond in VWF CK domain reported in the literatures

	Disulfide bond	Mutation	Phenotype	Reference
Intrachain	Cys2724-Cys2774	C2724Y	Type 3 VWD	This paper
	Cys2739-Csy2788	C2739Y	Type 3 VWD	[5]
	Cys2750-Csy2804	C2804Y	Type 3 VWD	[6]
	Cys2754-Cys2806	C2754W, C2806R	Type 3 VWD	[7,8,9]
Interchain	Cys2771-Cys2773’	C2771S/C2771Y, C2773S	Type 2 A/IID VWD	[13,14,15]
	Cys2771’-Cys2773	C2771S/C2771Y, C2773S	Type 2 A/IID VWD	[13,14,15]
	Cys2811-Cys2811’	C2811A	Normal VWF multimerization and secretion, but occurrence of odd-numbered multimer	[15,16,17]

ISSN: 1477-9560