Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

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

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Varughese, K. I.
  • Ruggeri, Zaverio
  • Celikel, R.

publication date

  • March 2004

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

abstract

  • The interaction between platelet glycoprotein (GP) Ib alpha and von Willebrand factor (VWF) is essential for thrombus formation, leading to the arrest of bleeding. The N-terminal domain of GP Ib alpha, which contains the binding sites for VWF and alpha-thrombin, crystallized in the tetragonal space group P4(3) with one molecule in the asymmetric unit. When the crystals were treated with platinum, the crystals changed their symmetry from tetragonal to monoclinic P2(1) 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 A resolution data.

subject areas

  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Platelet Glycoprotein GPIb-IX Complex
  • Platinum
  • Protein Binding
  • Protein Structure, Tertiary
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444903026805

PubMed ID

  • 14993663
scroll to property group menus

Additional Document Info

start page

  • 405

end page

  • 411

volume

  • 60

issue

  • Pt 3

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support