1qyy | pdb_00001qyy
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Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution
Overview
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.
Disease
Known diseases associated with this structure: Bernard-Soulier syndrome, type A OMIM:[606672], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[606672], von Willebrand disease, platelet-type OMIM:[606672]
About this Structure
1QYY is a Single protein structure of sequence from Homo sapiens with NAG and PT as ligands. Full crystallographic information is available from OCA.
Reference
Platinum-induced space-group transformation in crystals of the platelet glycoprotein Ib alpha N-terminal domain., Varughese KI, Ruggeri ZM, Celikel R, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):405-11. Epub 2004, Feb 25. PMID:14993663
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