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Blood, Vol. 111, Issue 3, 1240-1247, February 1, 2008
The tertiary structure and domain organization of coagulation factor VIII
Blood Shen et al.
111: 1240
Supplemental materials for: Shen et al
Files in this Data Supplement:
- Figure S1. Ramachandran Plot for factor VIIIa (JPG, 36.3 KB)
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96% of the residues are within allowed regions of the Ramachandran plot; 47 (4%) of the residues fall in disallowed regions. The vast majority of these residues are in poorly ordered surface loops in the A1 and A2 domains of the heavy chain.
- Figure S2. Rwork and Rfree values for structures from 3.5 to 3.9 Å resolution (JPG, 23.5 KB)
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The Rwork and Rfree values for factor VIII (horizontal lines), at 3.7 Å resolution, are 0.289 / 0.341. The individual values of Rwork and Rfree for 78 structures between 3.5 and 3.9 Å resolution, and their averages, are shown in the scatter plot.
- Figure S3. Copper binding at A1-A3 interfaces (JPG, 128 KB)
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Location of bound copper ions and their amino acid ligands in the A1-A3 interface of ceruloplasmin, factor VIII and factor V. The orientations of the domains are taken from the superposition shown in Figure 3.
- Figure S4. Binding epitopes for fVIII neutralizing antibody inhibitors (JPG, 151 KB)
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Left: The various sites that are known to act as epitopes for neutralizing antibodies are labeled and colored yellow; those in parentheses are found in regions that are not observed in the crystal structure, due to disorder. Right: The protein is color-coded using a spectrum corresponding to magnitude of crystallographic b-factors: blue regions display low b-factors, ranging up to red for the largest values (range of B-factors approximately 20 to 200 Å2).
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