Thrombin interaction with platelet membrane glycoprotein Ibα

被引：27

作者：

Adam, F ^{[1
]}

Bouton, MC ^{[1
]}

Huisse, MG ^{[1
]}

Jandrot-Perrus, M ^{[1
]}

机构：

[1] Univ Paris 07, INSERM, F-75870 Paris 18, France

来源：

TRENDS IN MOLECULAR MEDICINE | 2003年 / 9卷 / 11期

关键词：

IX-V COMPLEX; CRYSTAL-STRUCTURE; BINDING SITE; ACTIVATION; GLYCOCALICIN; AGGREGATION; ADHESION; PATHWAY;

D O I：

10.1016/j.molmed.2003.09.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction of thrombin with platelet glycoprotein Ibalpha (GPIbalpha) is required for optimal platelet activation. The crystal structures of platelet GPIbalpha bound to thrombin reported by Dumas et al. and Celikel et al. both reveal the simultaneous interaction of GPIbalpha with thrombin exosites I and II but differ markedly regarding how the two proteins interact. The possible consequences on thrombus formation of thrombin interacting with GPIbalpha are discussed in light of these new data.

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收藏

页码：461 / 464

页数：4

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