Figure 2.
Figure 2. Comparison of dormant human and Sfmoesin structures.
(a) The human FERM–C-terminal domain complex (PDB code 1EF1).
The three lobes of the ERM domain (F1, F2 and F3) are colored
cyan and the C-terminal domain is colored red. The β1 strand
of the C-terminal domain is contributed by a crystal-packing
interaction. (b) The 2.1 Å Sfmoesin structure. The
α-helical domain (yellow) folds into three extended helices
(αA, αB and αC), each containing elements that pack against
the FERM domain. The αB and αC helices form an anti-parallel
coiled-coil. (c) In the 3.0 Å structure, 67 more residues
of the vert,
similar 70 Å αB/αC coiled-coil are revealed. Figure
2. Comparison of dormant human and Sfmoesin structures. (a) The
human FERM–C-terminal domain complex (PDB code 1EF1). The
three lobes of the ERM domain (F1, F2 and F3) are colored cyan
and the C-terminal domain is colored red. The β1 strand of the
C-terminal domain is contributed by a crystal-packing
interaction. (b) The 2.1 Å Sfmoesin structure. The
α-helical domain (yellow) folds into three extended helices
(αA, αB and αC), each containing elements that pack against
the FERM domain. The αB and αC helices form an anti-parallel
coiled-coil. (c) In the 3.0 Å structure, 67 more residues
of the [3]not, vert, similar 70 Å αB/αC coiled-coil are
revealed.
vert,
similar 70 Å αB/αC coiled-coil are revealed. Figure
2. Comparison of dormant human and Sfmoesin structures. (a) The
human FERM–C-terminal domain complex (PDB code 1EF1). The
three lobes of the ERM domain (F1, F2 and F3) are colored cyan
and the C-terminal domain is colored red. The β1 strand of the
C-terminal domain is contributed by a crystal-packing
interaction. (b) The 2.1 Å Sfmoesin structure. The
α-helical domain (yellow) folds into three extended helices
(αA, αB and αC), each containing elements that pack against
the FERM domain. The αB and αC helices form an anti-parallel
coiled-coil. (c) In the 3.0 Å structure, 67 more residues
of the [3]not, vert, similar 70 Å αB/αC coiled-coil are
revealed.