Figure 4
Figure 4. The tetramer structure of GPIbβEabc shows a binding interface between GPIbβE-derived C-terminal cap region and GPIXE-derived convex loops. (A) Cartoon diagram showing 2 views of the GPIbβEabc tetramer structure related by a 90-degree rotation. The N-termini (N) of the molecules are at the peripheral of the tetramer, and the C-termini (C) are all located in proximity at the bottom of the lower panel. Sequences derived from GPIbβE are colored in blue and those derived from GPIXE in magenta. The side chain of GPIbβ-Tyr106 at each interface is shown in green as stick. (B) A close-up view of the interface between 2 GPIbβEabc molecules (GPIbβE-derived residues in blue and GPIXE-derived residues in magenta). Interacting side chains are labeled and colored accordingly, and underlined residues were subject to mutagenesis.

The tetramer structure of GPIbβEabc shows a binding interface between GPIbβE-derived C-terminal cap region and GPIXE-derived convex loops. (A) Cartoon diagram showing 2 views of the GPIbβEabc tetramer structure related by a 90-degree rotation. The N-termini (N) of the molecules are at the peripheral of the tetramer, and the C-termini (C) are all located in proximity at the bottom of the lower panel. Sequences derived from GPIbβE are colored in blue and those derived from GPIXE in magenta. The side chain of GPIbβ-Tyr106 at each interface is shown in green as stick. (B) A close-up view of the interface between 2 GPIbβEabc molecules (GPIbβE-derived residues in blue and GPIXE-derived residues in magenta). Interacting side chains are labeled and colored accordingly, and underlined residues were subject to mutagenesis.

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