|
Figure 1.
Figure 1. Overall Structure of the RyR NTD
(A) Overall
fold of the RyR2 NTD, showing the α helix (α1) and 3[10] helix
(3[10]h1) in red, β strands in blue, and loops in white. Two
views are shown (labeled “front” and “back”), rotated
180° around a vertical axis. All β strands are labeled for
reference. Loops present in the construct but not modeled are
shown as dotted lines. W98 in the α1-β5 loop is shown in stick
representation. The positions of the amino- and carboxytermini
are indicated.
(B) Sequence alignment of the NTD of mouse
RyR2, rabbit RyR1, and human RyR3. Conserved residues are
highlighted in gray. Secondary structure elements are shown on
top (RyR2) and at the bottom (RyR1). Sequence stretches present
in the constructs but not modeled in the electron density are
shown as dotted lines. Positions found in disease mutations are
marked with an asterisk and highlighted in red.
(C)
Superposition of the backbone trace of RyR1 (green) and RyR2 NTD
(blue). Loops with conformational changes are highlighted. The
view is the same as the front view of Figure 1A.
|
