Fig. 6: Dynamic residues in TPX2α5-α7 bound to MTs. | Nature Communications

Fig. 6: Dynamic residues in TPX2α5-α7 bound to MTs.

From: Structural basis of protein condensation on microtubules underlying branching microtubule nucleation

Fig. 6

a, b Representative aliphatic (a) and aromatic (b) regions of the 2D 13C-13C CORD spectra of U-[13C,15N]-TPX2α5-α7/MTs, acquired with 200 ms mixing time at 3 °C (teal) and 15 °C (gray). Representative intra- and inter-residue correlations observed exclusively at 3 °C are colored teal. The contacts present at 15 °C are labeled in black. The spectra were acquired at 14.1 T; the MAS frequency was 14 kHz. c The contacts involving dynamic residues mapped onto the structure of TPX2α5-α7. Contacts that are absent at 15 °C are shown as teal dashed lines; the corresponding dynamic residues are colored in orange. The zoom-in view shows representative hydrophobic residues that are more dynamic at higher temperature. d Expanded view of the TPX2α5-α7 structure showing the aromatic residues (purple) in the core. The cross peaks for these residues are absent at 15 °C suggesting greater mobility at higher temperature and different/heterogeneous sidechain orientations.

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