Figure 4.
Crystallization of Nb2 and GPVI. (A) Structure of Nb2 binding to GPVI. (i) Side view of the GPVI-Nb2 structure. (ii) Top-down view illustrating the domain swap hinge region. A cartoon representation is shown below each figure. Separate GPVI protein subunits are shown in green and cyan, and both Nb2 proteins are shown in yellow and pink. The domain-swapped D2 domains are labeled D2a and D2b for the N- and C-terminal D2 regions, respectively. (B) Comparison of the D2 domains from the non–domain-swapped structure (PDB: 2GI7) (i) and the domain-swapped structure (ii) with major features highlighted. This highlights the differences within the C-C′ hinge region, the C′ β-strand where no electron density was observed for the domain-swapped structure, and the presence of a 310 helix between βE and F. (C) Enlarged view of the D2 domain-swapped hinge region with the hinge loops colored in green and cyan and the interchain polar contacts, which stabilize this region, shown as red dashes.

Crystallization of Nb2 and GPVI. (A) Structure of Nb2 binding to GPVI. (i) Side view of the GPVI-Nb2 structure. (ii) Top-down view illustrating the domain swap hinge region. A cartoon representation is shown below each figure. Separate GPVI protein subunits are shown in green and cyan, and both Nb2 proteins are shown in yellow and pink. The domain-swapped D2 domains are labeled D2a and D2b for the N- and C-terminal D2 regions, respectively. (B) Comparison of the D2 domains from the non–domain-swapped structure (PDB: 2GI7) (i) and the domain-swapped structure (ii) with major features highlighted. This highlights the differences within the C-C′ hinge region, the C′ β-strand where no electron density was observed for the domain-swapped structure, and the presence of a 310 helix between βE and F. (C) Enlarged view of the D2 domain-swapped hinge region with the hinge loops colored in green and cyan and the interchain polar contacts, which stabilize this region, shown as red dashes.

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