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. 2001 Apr 24;98(9):4955–4960. doi: 10.1073/pnas.091083898

Table 4.

Manipulation of conformational equilibria

Design Variant Kd Zn, μM
A* 5.1  ± 0.2
K15IIA 1.0  ± 0.1
E111IM 1.0  ± 0.1
K15IIA + E111IM 1.0  ± 0.2
A* I329F 0.35  ± 0.04

Residues K15 and E111 are residues that form hydrogen bonds with maltose in the wild-type receptor. Removal of these vestigial interactions is intended to favor formation of the closed state. Residue 329 is located in the hinge region. Mutation I329F is intended to destabilize the open state. Subscript indicates the domain in which a residue is located (see Fig. 1). Residue 329 is located in the hinge region.