1M10

Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain

Summary for 1M10

• Entry DOI: 10.2210/pdb1m10/pdb
• Related: 1M0Z
• Descriptor: von Willebrand Factor, Glycoprotein Ib alpha (2 entities in total)
• Functional Keywords: leucine-rich repeat, hemostasis, dinucleotide binding fold, blood clotting
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P04275; Membrane; Single-pass type I membrane protein: P07359
• Total number of polymer chains: 2
• Total formula weight: 56066.29

Authors

Huizinga, E.G.,Tsuji, S.,Romijn, R.A.P.,Schiphorst, M.E.,de Groot, P.G.,Sixma, J.J.,Gros, P. (deposition date: 2002-06-16, release date: 2002-08-28, Last modification date: 2024-10-16)

Primary citation

Huizinga, E.G.,Tsuji, S.,Romijn, R.A.,Schiphorst, M.E.,de Groot, P.G.,Sixma, J.J.,Gros, P.
Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.
Science, 297:1176-1179, 2002

PubMed Abstract: Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites of vascular damage and play a role in haemostasis and thrombosis. Here we present structures of the GpIbalpha amino-terminal domain and its complex with the VWF domain A1. In the complex, GpIbalpha wraps around one side of A1, providing two contact areas bridged by an area of solvated charge interaction. The structures explain the effects of gain-of-function mutations related to bleeding disorders and provide a model for shear-induced activation. These detailed insights into the initial interactions in platelet adhesion are relevant to the development of antithrombotic drugs.

PubMed: 12183630
DOI: 10.1126/science.107355

Experimental method

X-RAY DIFFRACTION (3.1 Å)