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Figure 4.
Figure 4. Extent and sequence conservation of the surfaces
buried by the α-helical domain and linker region. (a) The
Sfmoesin FERM domain. The view is rotated by  vert,
similar 180° around a vertical axis from that in Figure 2.
(b) Molecular surface of the FERM domain. Yellow regions are
those in contact with the α-helical domain and linker region (
vert,
similar 1800 Å^2 of buried accessible surface area). (c)
Conservation of the FERM domain. Magenta regions correspond to
residues that are either identical or substituted conservatively
(e.g. Asp/Glu, Arg/Lys, Ser/Thr) in all ERM-merlin proteins.
Green regions correspond to residues conserved only in the ERM
family. Figure 4. Extent and sequence conservation of the
surfaces buried by the α-helical domain and linker region. (a)
The Sfmoesin FERM domain. The view is rotated by [3]not, vert,
similar 180° around a vertical axis from that in [4]Figure
2. (b) Molecular surface of the FERM domain. Yellow regions are
those in contact with the α-helical domain and linker region (
[5]not, vert, similar 1800 Å^2 of buried accessible
surface area). (c) Conservation of the FERM domain. Magenta
regions correspond to residues that are either identical or
substituted conservatively (e.g. Asp/Glu, Arg/Lys, Ser/Thr) in
all ERM-merlin proteins. Green regions correspond to residues
conserved only in the ERM family.
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