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Figure 1.
Structure of the human thrombin mutant D102N in complex with
the extracellular fragment of human PAR1. (A) Thrombin is
rendered in surface representation (wheat) with residues <4
Å from the bound fragment of PAR1 (stick model) colored in
light blue. The orientation is centered on the 30-loop that
separates exosite I on the right from the active site cleft on
the left. The 60-loop occupies the upper rim of the active site.
The electron density 2F[o] − F[c] map (green mesh) is
contoured at 1.0σ. (B) Details of the molecular contacts at the
thrombin–PAR1 interface, with hydrophobic regions of the
thrombin epitope colored in orange and polar regions colored in
light blue. H bonds are depicted as broken lines. Residues
involved in contacts <4 Å are listed in Table 1 and are
labeled in black for thrombin and red for PAR1. The
extracellular fragment of PAR1 engages exosite I through polar
and hydrophobic interactions.
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