GP1BA

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein receptor composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds.^[5] The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V to form the glycoprotein Ib-IX-V complex. Binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury,^[6] and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis.^[7] This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard–Soulier syndromes and platelet-type von Willebrand disease.^[8]

GP1BA has been shown to interact with YWHAZ^[9][10][11] and FLNB.^[12]

CCP-224, a short PEG-conjugated form of the cyclic peptide OS-1, binds to human GPIb alpha with high affinity and can prevents neutrophil-platelet aggregation in Sickle Cell Disease.^[13] In vivo, platelet-mediated thrombus formation can be greatly reduced in arterioles of mice, injured by laser, following an infusion of the OS-1 peptide.^[14] The OS-1 peptide prevents binding of GPIb alpha to the VWF A1 domain.^[15] The co-crystal structure of GPIb alpha and OS-1 has been reported.^[16]

• Cluster of differentiation