 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](ba5090fig3mag.jpg)
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Figure 3
Flexible versus rigid-body recognition. (a) Chymotrypsin–ovomucoid: the protease surface in contact with the inhibitor (1cho ; Fujinaga et al., 1987  ) is viewed through the inhibitor main chain. This complex illustrates rigid-body recognition. It has a high affinity (Kd ≃ 10−11 M), a standard-size interface (B = 1470 Å2) in a single patch and a low Cα r.m.s.d. between the free and bound components (0.6 Å). (b) Transducin: the surface of the Gα subunit that interacts with the Gβγ pair of subunits is viewed through the Gβγ main chain (PDB code 1got
; Lambright et al., 1996). Transducin illustrates flexible recognition; the Gα–Gβγ interface is large (B = 2500 Å2), in two patches, and the association involves major conformation changes (1.8 Å Cα r.m.s.d.) in both Gα and Gβγ; the affinity is comparatively low (Kd ≃ 10−7 M). |
![[Figure 3]](ba5090fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
