1P9A

Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution

Summary for 1P9A

• Entry DOI: 10.2210/pdb1p9a/pdb
• Related: 1OOK
• Descriptor: Platelet glycoprotein Ib alpha chain precursor, beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: platelet receptors, glycocalicin, leucine rich repeats, blood clotting
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P07359
• Total number of polymer chains: 1
• Total formula weight: 33055.47

Authors

Varughese, K.I.,Celikel, R.,Ruggeri, Z.M. (deposition date: 2003-05-09, release date: 2003-07-22, Last modification date: 2024-04-03)

Primary citation

Celikel, R.,McClintock, R.A.,Roberts, J.R.,Mendolicchio, G.L.,Ware, J.,Varughese, K.I.,Ruggeri, Z.M.
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha
Science, 301:218-221, 2003

PubMed Abstract: Thrombin bound to platelets contributes to stop bleeding and, in pathological conditions, may cause vascular thrombosis. We have determined the structure of platelet glycoprotein Ibalpha (GpIbalpha) bound to thrombin at 2.3 angstrom resolution and defined two sites in GpIbalpha that bind to exosite II and exosite I of two distinct alpha-thrombin molecules, respectively. GpIbalpha occupancy may be sequential, as the site binding to alpha-thrombin exosite I appears to be cryptic in the unoccupied receptor but exposed when a first thrombin molecule is bound through exosite II. These interactions may modulate alpha-thrombin function by mediating GpIbalpha clustering and cleavage of protease-activated receptors, which promote platelet activation, while limiting fibrinogen clotting through blockade of exosite I.

PubMed: 12855810
DOI: 10.1126/science.1084183

Experimental method

X-RAY DIFFRACTION (1.7 Å)