Platinum-induced space-group transformation in crystals of the platelet glycoprotein Ib alpha N-terminal domain.
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.
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. kiv@scripps.edu
Kottayil I
KI
Varughese
Zaverio M
ZM
Ruggeri
Reha
R
Celikel
D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000737:chemistry* / Q000378:metabolism*; D010984:Platinum / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D019038:Platelet Glycoprotein GPIb-IX Complex; D010984:Platinum