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Fig. 1 | Experimental Hematology & Oncology

Fig. 1

From: The GPIb-IX complex on platelets: insight into its novel physiological functions affecting immune surveillance, hepatic thrombopoietin generation, platelet clearance and its relevance for cancer development and metastasis

Fig. 1

Structure of GPIb-IX. The largest subunit of the complex is GPIbα, which consists of a N-terminal binding domain (made up of 8 leucine-rich repeats), a negatively charged domain, a sialomucin region (macroglycopeptide domain), the mechanosensitive domain (MSD), and proximal to the membrane, the trigger sequence. Intracellularly, GPIbα interacts with protein 14-3-3ζ and filamin A which links the complex to the cytoskeleton. The transmembrane domain provides a close interaction with GPIbβ and GPIX to form a stable parallel four-helical bundle structure. This complex structure is further strengthened by the interplay of GPIbβ and GPIX extracellular domains with the MSD in GPIbα. GPV is weakly associated with GPIb-IX by polar interactions and can be replaced by other receptors

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Experimental Hematology & Oncology

ISSN: 2162-3619

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