1QYY

Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution

Summary for 1QYY

• Entry DOI: 10.2210/pdb1qyy/pdb
• Related: 1OOK 1P9A
• Descriptor: Platelet glycoprotein Ib alpha chain, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, PLATINUM (II) ION, ... (5 entities in total)
• Functional Keywords: platelet receptors, glycocalicin, leucine rich repeats, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P07359
• Total number of polymer chains: 2
• Total formula weight: 66168.70

Authors

Varughese, K.I.,Ruggeri, Z.M.,Celikel, R. (deposition date: 2003-09-12, release date: 2004-03-02, Last modification date: 2024-11-13)

Primary citation

Varughese, K.I.,Ruggeri, Z.M.,Celikel, R.
Platinum-induced space-group transformation in crystals of the platelet glycoprotein Ib alpha N-terminal domain.
Acta Crystallogr.,Sect.D, 60:405-411, 2004

PubMed 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.

PubMed: 14993663
DOI: 10.1107/S0907444903026805

Experimental method

X-RAY DIFFRACTION (2.8 Å)