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Figure 3.
Crystal structure of the SC-(1-325)·bovineα-thrombin
complex. The thrombin moiety is shown as a solid surface colored
according to the electrostatic surface potential, from strongly
negative (deep red) to strongly positive (deep blue). The
boomerang-shaped SC molecule is comprised of the N-terminal
domain D1 (helices α[1]^D1 to α[3]^D1) and the C-terminal
domain D2 (helices α[1]^D2 to α[6]^D2) and is represented as a
green ribbon. The anion-binding exosite I, the active site
(Ser^195), and the 148 loop (Trp^148) of bovine α-thrombin are
labeled. The N terminus of SC (defined from ^SCSer^7 onwards) is
placed close to the Ile^16 activation pocket of thrombin but is
disordered in the complexes with bovine and human thrombin and
extends away from the enzyme surface.
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