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Science 11 July 2003:
Vol. 301. no. 5630, pp. 177 - 179
DOI: 10.1126/science.1087734

Perspectives

STRUCTURAL BIOLOGY:
A Ménage à Trois in Two Configurations

J. Evan Sadler

The interaction of thrombin with the GpIb-IX-V complex on the surface of platelets is crucial for the formation of blood clots following vascular injury. In a Perspective, Sadler discusses two new crystallographic studies (Celikel et al., Dumas et al.) that shed new but perhaps conflicting light on this vital interaction.


The author is at the Howard Hughes Medical Institute, Department of Medicine and Department of Biochemistry and Molecular Biophysics, Washington University, St. Louis, MO 63110, USA. E-mail: esadler{at}im.wustl.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Thrombin Mutant W215A/E217A Acts as a Platelet GPIb Antagonist.
M. A. Berny, T. C. White, E. I. Tucker, L. A. Bush-Pelc, E. Di Cera, A. Gruber, and O. J.T. McCarty (2008)
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Detection and Purification of Tyrosine-sulfated Proteins Using a Novel Anti-sulfotyrosine Monoclonal Antibody.
A. J. Hoffhines, E. Damoc, K. G. Bridges, J. A. Leary, and K. L. Moore (2006)
J. Biol. Chem. 281, 37877-37887
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Glycoprotein Ib{alpha}-Mediated Platelet Adhesion and Aggregation to Immobilized Thrombin Under Conditions of Flow.
C. Weeterings, J. Adelmeijer, T. Myles, P. G. de Groot, and T. Lisman (2006)
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Directing thrombin.
D. A. Lane, H. Philippou, and J. A. Huntington (2005)
Blood 106, 2605-2612
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Effects of Thrombin on Interactions Between {beta}3-Integrins and Extracellular Matrix in Platelets and Vascular Cells.
G.A. Stouffer and S.S. Smyth (2003)
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