American Society of Hematology

Figure 3

$Figure 3. Comparisons of fV and fVIII structures. The relative domain orientations of r-fVIII with a previously reported model generated from electron diffraction studies, and with 2.8-Å resoloution crystal structures of ceruloplasmin and of an inactive (A2-deleted) fV construct are shown. The structures are all oriented similarly with respect to the A domains. Metals ions modeled in the various structures as calcium and copper are indicated as yellow and blue spheres, respectively. The docked orientations of the C domains of r-fVIII, and their interactions with each other and with the A3 domain of the light chain, are both rotated by approximately 90° with respect to the electron diffraction model, but in excellent agreement with their homologous domains in fV. The box shows superposition of full-length fVIII (colored by domains) versus inactive (A2-deleted) fV (shown in orange). The RMSD for aligned α-carbons is approximately 2 Å.$

Comparisons of fV and fVIII structures. The relative domain orientations of r-fVIII with a previously reported model generated from electron diffraction studies, and with 2.8-Å resoloution crystal structures of ceruloplasmin and of an inactive (A2-deleted) fV construct are shown. The structures are all oriented similarly with respect to the A domains. Metals ions modeled in the various structures as calcium and copper are indicated as yellow and blue spheres, respectively. The docked orientations of the C domains of r-fVIII, and their interactions with each other and with the A3 domain of the light chain, are both rotated by approximately 90° with respect to the electron diffraction model, but in excellent agreement with their homologous domains in fV. The box shows superposition of full-length fVIII (colored by domains) versus inactive (A2-deleted) fV (shown in orange). The RMSD for aligned α-carbons is approximately 2 Å.

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