Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain
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.
- Authors:
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI Identifier:
- 1252784
- Alternate Identifier(s):
- OSTI ID: 1629218
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Journal Article: Published Article
- Journal Name:
- Data in Brief
- Additional Journal Information:
- Journal Name: Data in Brief Journal Volume: 7 Journal Issue: C; Journal ID: ISSN 2352-3409
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; von Willebrand factor; von Willebrand disease; Protein crystallization; Platelet adhesion
Citation Formats
Campbell, James C., Tischer, Alexander, Machha, Venkata, Moon-Tasson, Laurie, Sankaran, Banumathi, Kim, Choel, and Auton, Matthew. Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain. United States: N. p., 2016.
Web. doi:10.1016/j.dib.2016.05.004.
Campbell, James C., Tischer, Alexander, Machha, Venkata, Moon-Tasson, Laurie, Sankaran, Banumathi, Kim, Choel, & Auton, Matthew. Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain. United States. https://doi.org/10.1016/j.dib.2016.05.004
Campbell, James C., Tischer, Alexander, Machha, Venkata, Moon-Tasson, Laurie, Sankaran, Banumathi, Kim, Choel, and Auton, Matthew. 2016.
"Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain". United States. https://doi.org/10.1016/j.dib.2016.05.004.
@article{osti_1252784,
title = {Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain},
author = {Campbell, James C. and Tischer, Alexander and Machha, Venkata and Moon-Tasson, Laurie and Sankaran, Banumathi and Kim, Choel and Auton, Matthew},
abstractNote = {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.},
doi = {10.1016/j.dib.2016.05.004},
url = {https://www.osti.gov/biblio/1252784},
journal = {Data in Brief},
issn = {2352-3409},
number = C,
volume = 7,
place = {United States},
year = {Wed Jun 01 00:00:00 EDT 2016},
month = {Wed Jun 01 00:00:00 EDT 2016}
}
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Works referencing / citing this record:
Glycosylation sterically inhibits platelet adhesion to von Willebrand factor without altering intrinsic conformational dynamics
journal, October 2019
- Tischer, Alexander; Machha, Venkata R.; Moon‐Tasson, Laurie
- Journal of Thrombosis and Haemostasis, Vol. 18, Issue 1
Platelet‐type von Willebrand disease: Local disorder of the platelet GPI bα β‐switch drives high‐affinity binding to von Willebrand factor
journal, September 2019
- Tischer, Alexander; Machha, Venkata R.; Moon‐Tasson, Laurie
- Journal of Thrombosis and Haemostasis, Vol. 17, Issue 12