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. 2022 Nov 10;41(24):e112440. doi: 10.15252/embj.2022112440

Figure 2. The AlphaFold predicted structure of CrIFT81/74/27/251–136/22.

Figure 2

  1. AlphaFold predicts the structure of IFT81/74128‐C/27/251–136/22 complex as two halves built on the IFT81/74 CC scaffold and hinged by a short loop region around the amino acids 460 of both IFT81 and IFT74. CrIFT22 binds near the hinge region on the CC domain VI (B) while the CrIFT27/25 heterodimer is docked proximal to the C‐termini of IFT81/74 in a ‘L‐shape’ structure formed by CCs VIII and IX.
  2. The top view of the complex shows the organization of the IFT81/74 CCs and the docking sites for IFT27/25 and IFT22.
  3. 3 independent AF models of the IFT81/74128‐C/27/251–136/22 complex are superimposed using their N‐terminal halves to illustrate high flexibility between the separate parts of IFT81/74.
  4. The predicted alignment error (PAE) plot for the model shown in panels A‐B. This plot assesses the confidence in the relative position of subunits within the complex. The Y‐ and the X‐axes show the residues indexed of the corresponding subunits as indicated. The aligned error in angstroms (Å) is color coded according to the bar to the right of the plot. Green color indicates low PAE (high confidence) and white color indicates high PAE (low confidence).