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Figure 1.
Figure 1. Secondary Structure of Htt17Q-EX1
(A) Amino
acid sequence of MBP-Htt17Q-EX1. MBP3A denotes the maltose
binding protein followed by a 3Ala linker. M371 to Q430 is the
sequence of Htt17Q-EX1, which is subdivided into a 17 aa
N-terminal region (M371 to F387), poly17Q region (Q388 to Q404),
poly11P region (P405 to P415), and 15 aa mixed P/Q region (Q416
to Q430). The sequence from Q431 to the C terminus is the 19 aa
tag added to facilitate crystallization.
(B) The structure
of Htt17Q-EX1 trimer from c^95 crystal. The structures of MBP
and 3A linker are removed for clarity. The amino-terminal α
helix of Htt17Q-EX1 extends from Met371 to Phe387 (Green). The
following poly17Q region (orange) is α helical and unstructured
(random coil). The poly11P region (blue) adopts a PP helix
(shown as stick model) in the kinked conformation. The initial
part of the polyP/Q region (purple) is also in PP-helix
conformation (shown as stick model). The terminal part of the
poly17Q region (orange) is in the extended conformation (shown
as stick model).
(C) The structure of Htt17Q-EX1 trimer
from c[Hg]^99 crystal. Same as in (B) but the poly11P region is
in the straight conformation.
(D) The complete structure of
B molecule of Htt17Q-EX1 monomer from c^95 crystal. The striped
orange loops are for the random coil region between Gln389 and
Gln399, which is invisible on the map.
(E) The complete
structure of A molecule of Htt17Q-EX1 monomer from c[Hg]^99
crystal. The striped orange loops are for the random coil region
between Gln391 and Gln398, which is invisible on the map.
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