Platinum-induced space-group transformation in crystals of the platelet glycoprotein Ibα N-terminal domain

Authors: Varughese, Kottayil I.; Ruggeri, Zaverio M.; Celikel, Reha

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 405-411(7)

Publisher: Blackwell Publishing

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Abstract:

The interaction between platelet glycoprotein (GP) Ibα and von Willebrand factor (VWF) is essential for thrombus formation, leading to the arrest of bleeding. The N-terminal domain of GP Ibα, which contains the binding sites for VWF and α-thrombin, crystallized in the tetragonal space group P4₃ with one molecule in the asymmetric unit. When the crystals were treated with platinum, the crystals changed their symmetry from tetragonal to monoclinic P2₁ with two molecules in the asymmetric unit. The structure of the monoclinic form was solved using two-wavelength platinum anomalous dispersion data. The tetragonal crystal structure was subsequently solved using molecular-replacement techniques using the monoclinic structure as the search model and was refined with 1.7 Å resolution data.

Keywords: platelet glycoproteins; blood clotting; leucine-rich repeats; space-group transformation

Document Type: Research article

DOI: 10.1107/S0907444903026805

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