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Figure 2.
Figure 2: Structural basis for VPS4 MIT recognition of
CHMP1–3. a, Alignments of ESCRT-III protein C termini.
C-terminal sequences of human proteins from the six CHMP classes
are shown explicitly, together with a graph showing the degree
of sequence conservation within aligned CHMP1–3 C termini (50
sequences; see Supplementary Table 2) and the consensus
sequence (below the graph). Note that ESCRT-III proteins of the
CHMP4–6 class do not conform to the consensus. b, Solution
structure of the VPS4A MIT–CHMP1A[180–196] complex, with the
three conserved CHMP1A[180–196] leucines shown explicitly.
This helical colour scheme is also used in c–f. c, Structure
of the VPS4A MIT–CHMP1A[180–196] complex. The MIT domain is
shown in a space-filling model with Leu 64 highlighted in blue;
important residues on both sides of the interface are shown
explicitly. Arrows denote the approximate orientations of the
three leucine-binding pockets shown in d–f. d–f, Close-up
views of the three leucine-binding pockets of the VPS4A MIT
domain showing the hydrophobic pocket views in detail, as well
as complementary charge interactions between Glu 184 and Arg 57
(d), between Arg 195 and Glu 37 (e), and between Arg 190 and Glu
68 (Asp 65) (f); CHMP1A residues are listed first.
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