 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](cb5036fig3mag.jpg)
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Figure 3
Activation of MPK38 by the UBA linker. (a) Superposition of the MPK38 (T167E) N-lobe (blue) and the MARK1 N-lobe (white). (b, c) Detailed interactions are shown among the KD αC helix, KD β4 and the UBA linker. The key residues that show conformational differences in the KDs of MPK38 and MARK1 are labelled. The distance between Glu in αC and Lys in β4 is shown. (d) Structures of MARK1 (left, white) and MPK38 (T167E) (right, blue) presented in different views to those in (b). The distance between Glu in αC and Lys in β4 is shown for both proteins (6.1 Å in MARK1 and 3.0 Å in MPK38). The ion pairs are displayed as red dashed lines. |
![[Figure 3]](cb5036fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
