Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain

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• 作者：James C. Campbell^a ; Alexander Tischer^b ; Venkata Machha^b ; Laurie Moon-Tasson^b ; Banumathi Sankaran^c ; Choel Kim^a ; ^d ; ^e ; Matthew Auton^b ; ^{auton.matthew@mayo.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：von Willebrand factor ; von Willebrand disease ; Protein crystallization ; Platelet adhesion
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：7
• 期：Complete
• 页码：1700-1706
• 全文大小：955 K

文摘

von Willebrand factor׳s (VWF) primary hemostatic responsibility is to deposit platelets at sites of vascular injury to prevent bleeding. This function is mediated by the interaction between the VWF A1 domain and the constitutively active platelet receptor, GPIbα. The crystal structure of the A1 domain harboring the von Willebrand disease (vWD) type 2M mutation p.Gly1324Ser has been recently published in the Journal of Biological Chemistry describing its effect on the function and structural stability of the A1 domain of VWF, “Mutational constraints on local unfolding inhibit the rheological adaptation of von Willebrand factor” [1]. The mutation introduces a side chain that thermodynamically stabilizes the domain by reducing the overall flexibility of the A1–GPIbα binding interface resulting in loss-of-function and bleeding due to the inability of A1 to adapt to a binding competent conformation under the rheological shear stress blood flow.

In this data article we describe the production, quality control and crystallization of the p.Gly1324Ser vWD variant of the A1 domain of VWF. p.Gly1324Ser A1 was expressed in Escherichia coli as insoluble inclusion bodies. After the preparation of the inclusion bodies, the protein was solubilized, refolded, purified by affinity chromatography and crystallized. The crystal structure of the p.Gly1324Ser mutant of the A1 domain is deposited at the Protein Data Bank PDB: 5BV8