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Figure 1.
Figure 1. Structures of KAP and PTP1B(A) Stereo view
showing a 2F[o]-F[c] electron density omit map contoured at 1σ
in the vicinity of the catalytic Cys residue (Cys-140) of
wild-type KAP revealing the formation of a disulphide bond to
Cys-79.(B) Ribbon diagram comparing KAPt with PTP1B. The PTP
loop of both molecules is shown in yellow, the acid/base loop
(WPD loop) in red, and the Q loop in white. The pTyr recognition
segment of PTP1B is in green. A sulfate ion and pTyr residue are
shown at the catalytic sites of KAPt and PTP1B, respectively.
Figures were created using AESOP (M. E. M. N., unpublished
data), BOBSCRIPT (Esnouf, 1997), and Raster3D (Merit and Murphy,
1994)
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