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

James Cambell, Alexander Tischer, Venkata Machha, Laurie Moon-Tasson, Banumathi Sankaran, Choel Kim, Matthew T Auton

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1700-1706
Number of pages7
JournalData in Brief
Volume7
DOIs
StatePublished - Jun 1 2016

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loss of function
inclusion
Disease
data bank
quality control
flexibility
chemistry
responsibility
interaction

Keywords

  • Platelet adhesion
  • Protein crystallization
  • Von Willebrand disease
  • Von Willebrand factor

ASJC Scopus subject areas

  • General
  • Education

Cite this

Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain. / Cambell, James; Tischer, Alexander; Machha, Venkata; Moon-Tasson, Laurie; Sankaran, Banumathi; Kim, Choel; Auton, Matthew T.

In: Data in Brief, Vol. 7, 01.06.2016, p. 1700-1706.

Research output: Contribution to journalArticle

Cambell, James ; Tischer, Alexander ; Machha, Venkata ; Moon-Tasson, Laurie ; Sankaran, Banumathi ; Kim, Choel ; Auton, Matthew T. / Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain. In: Data in Brief. 2016 ; Vol. 7. pp. 1700-1706.
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AU - Kim, Choel

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