Figure 8.

HCII 1-75 molecular model. (A) Molecular model of HCII residues 1-75. HCII 1-75 is shown in ribbon representation (purple) and corresponding space filling model (grey). Helices are labeled 1, 2 and 3 corresponding to residues 4-12, 26-36 and 60-67 of HCII, respectively. (B) Structural superimposition of helix 3 (purple) from the HCII 1-75 molecular model with the same region of HCII (yellow) observed in the apo-HCII crystal structure (PDB 1JMJ). HCII subunits are labeled HCIIa and HCIIb and colored green and cyan, respectively. Amino acid residues of HCII included in the structural alignment are labeled. (C) Structural superimposition of HCII 1-75 molecular model with the HCII-thrombin encounter complex determined by x-ray crystallography (PDB 1JMO). HCII, light green; HCII residues 54-73 are shown in yellow; thrombin, cyan; HCII 1-75, purple; acidic residues used for structural alignment are shown in stick. Stereogram images are shown in all cases.

Boyle et al. BMC Biochemistry 2013 14:6   doi:10.1186/1471-2091-14-6
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