Varughese Kottayil I, Ruggeri Zaverio M, Celikel Reha
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):405-11. doi: 10.1107/S0907444903026805. Epub 2004 Feb 25.
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.
血小板糖蛋白（GP）Ibα与血管性血友病因子（VWF）之间的相互作用对于血栓形成至关重要，可导致出血停止。GP Ibα的N端结构域包含VWF和α-凝血酶的结合位点，以四方晶系空间群P4(3)结晶，不对称单元中有一个分子。当晶体用铂处理时，晶体的对称性从四方晶系变为单斜晶系P2(1)，不对称单元中有两个分子。利用双波长铂反常散射数据解析了单斜晶系的结构。随后，以单斜晶系结构为搜索模型，采用分子置换技术解析了四方晶系晶体结构，并用1.7 Å分辨率的数据进行了精修。
