Exploring binding sites other than the catalytic core in the crystal structure of the catalytic domain of MKP-­4

Jeong, D.G.; Yoon, T.S.; Jung, S.-K.; Park, B.C.; Park, H.; Ryu, S.E.; Kim, S.J.

doi:10.1107/S0907444910042381

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 1
Crystal structure of MKP-4C. (a) Ribbon representation of the catalytic domain of MKP-4. Secondary-structural boundaries are α1, 222–228; α2, 268–282; α3, 295–309; α4, 311–323; α5, 331–346; β1, 205–208; β2, 211–214; β3, 232–237; β4, 243–246; β5, 251–255; β6, 285–289. (b) Comparison of C^α traces. The C^α trace of MKP-4C (black) is superimposed on that of MKP-5C (red). Superposition was performed with the program O (Jones et al., 1991

) using a criterion of less than 3.8 Å for more than three consecutive C^α atoms. The regions that significantly deviate are labelled on the drawing. PTP, PTP-loop; GA, general acid loop.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 67| Part 1| December 2011| Pages 25-31

doi:10.1107/S0907444910042381

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