|
Figure 5.
Figure 5. The N-terminal HEAT Repeats of Cand1 Interact
with a Conserved Surface Cleft of the Cul1 CTD and Bury the Cul1
Neddylation Site Lysine Residue(A) Interactions between the
first two Cand1 HEAT repeats and the Cul1 CTD surface cleft. The
molecular surfaces of Cul1 and Roc1 are colored in green and
red. Surfaces of conserved Cul1 residues are shown in yellow.
Important structural elements of the proteins are labeled.(B)
Closeup view of the interfaces among the Cul1 WH-B domain,
Cand1's first HEAT repeat, and the Roc1 RING domain. Residues
interacting with Cul1 Lys720, as well as several surrounding
amino acids, are shown.(C) Zoomed-out view of (B) with surface
representation. The ε-amino group of the Cul1 Lys720 residue is
completely buried and invisible. Cul1 residues conserved among
all human cullins are colored in yellow. The surface of three
such conserved Cul1 residues located on the opposite side of the
Cul1 WH-B domain where the Cand1-interacting surface cleft is
found are indicated. This surface area represents a potential
site on the Cul1 CTD for interacting with additional regulatory
factors.
|
