Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα

Reha Celikel, Richard A. McClintock, James R. Roberts, G. Loredana Mendolicchio, Jerry Ware, Kottayil I. Varughese, Zaverio M. Ruggeri

Research output: Contribution to journalArticlepeer-review


Thrombin bound to platelets contributes to stop bleeding and, in pathological conditions, may cause vascular thrombosis. We have determined the structure of platelet glycoprotein Ibα (GpIbα) bound to thrombin at 2.3 angstrom resolution and defined two sites in GpIbα that bind to exosite II and exosite I of two distinct α-thrombin molecules, respectively. GpIbα occupancy may be sequential, as the site binding to α-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 α-thrombin function by mediating GpIbα clustering and cleavage of protease-activated receptors, which promote platelet activation, while limiting fibrinogen clotting through blockade of exosite I.

Original languageEnglish
Pages (from-to)218-221
Number of pages4
Issue number5630
Publication statusPublished - Jul 11 2003

ASJC Scopus subject areas

  • General


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