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

Authors
  • Campbell, James C1
  • Tischer, Alexander2
  • Machha, Venkata2
  • Moon-Tasson, Laurie2
  • Sankaran, Banumathi3
  • Kim, Choel4
  • Auton, Matthew2
  • 1 Structural and Computational Biology and Molecular Biophysics Program, Baylor College of Medicine, Houston, TX, USA.
  • 2 Division of Hematology, Departments of Internal Medicine and Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN, USA.
  • 3 Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, BLDG 6R2100, Berkeley, CA, USA.
  • 4 Structural and Computational Biology and Molecular Biophysics Program, Baylor College of Medicine, Houston, TX, USA; Department of Pharmacology, Baylor College of Medicine, Houston, TX, USA; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
Type
Published Article
Journal
Data in Brief
Publisher
Elsevier
Publication Date
Jun 01, 2016
Volume
7
Pages
1700–1706
Identifiers
PMID: 27761512
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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.

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