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Figure 2.
Solution structure of the TZF12 domain in human MBNL2. (A)
Stereo-view of the best 20 structures of the TZF12 domain
(residues Val8-Asn82). ZF1 and ZF2 of TZF12 are colored
aquamarine and coral, respectively. (B) Ribbon presentation of
the lowest energy structure of the TZF12 domain. The colors for
the backbones of ZF1 and ZF2 are the same as in A. The side
chains of the ligand residues and the zinc ions are shown in
yellow and gray, respectively. The side chains of the
hydrophobic residues that constitute the hydrophobic core of
TZF12 are shown in green. The ribbon diagram in the right panel
is rotated horizontally by 90[deg] from that on the left. (C)
Ribbon diagrams of TZF12 with the side chains of the positively
charged and aromatic residues of ZF1 (left panel) and ZF2 (right
panel), which are shown in blue and magenta, respectively. (D)
Electrostatic surface potential of the TZF12 domain. The blue
and red colors represent positive and negative electrostatic
surface potential, respectively. (E) Hydrophobic and positively
charged surface residues of the TZF12 domain. In C, D, and E,
the ZF1 and ZF2 surface orientations (left and right panel) were
obtained by 45[deg] and [minus sign]45[deg] vertical rotations
of the ribbon structure on the left in B. The ribbon diagrams
(C), the electrostatic potential (D), and the hydrophobic
surfaces (E) have the same orientation. The cyan and red
ellipses on the surfaces (D, E) of TZF12 mark the pockets formed
by the conserved residues. The red ellipse marks the pocket that
results from the formation of a compact global fold with the
tandem zinc fingers.
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