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

Journal Article · Wed Jun 01 00:00:00 EDT 2016 · Data in Brief

DOI:https://doi.org/10.1016/j.dib.2016.05.004· OSTI ID:1252784

Campbell, James C.; Tischer, Alexander; Machha, Venkata; Moon-Tasson, Laurie; Sankaran, Banumathi; Kim, Choel; Auton, Matthew

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.

• Research Organization: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
• Sponsoring Organization: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
• Grant/Contract Number: AC02-05CH11231
• OSTI ID: 1252784
• Alternate ID(s): OSTI ID: 1629218
• Journal Information: Data in Brief, Journal Name: Data in Brief Vol. 7 Journal Issue: C; ISSN 2352-3409
• Publisher: Elsevier
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
von Willebrand factor
von Willebrand disease
Protein crystallization
Platelet adhesion