Figure 3.
Figure 3 Shadow domain alignment in which the residues involved
in complex formation are highlighted (numbering is for mouse HP1
).
Residues important for recognition of the PXVXL motif are
highlighted in yellow (Val-224) and red (Pro-222/Leu-226 at the
-2/+2 positions). Residues that form the hydrophobic patch that
interacts with the flanking N- and C-terminal sequences
(Phe-217/Ile-218 and Ile-229/Leu-230 at the -6/-7 and +5/+6
positions, respectively) are highlighted in blue. Residues that
are not conserved and are predicted to alter specificity are
boxed. Conserved residues that define the fold of the shadow
domain are highlighted in grey, while residues important for
dimerisation are indicated by blue triangles. Phe-163 (indicated
by a green dot) is important for both the structure of the
shadow domain and peptide binding. The positions of secondary
structure elements in mouse HP1 are
indicated by purple arrows ( -strands)
and cylinders ( -helices)--the
dots indicate the positions of the conserved bulges in the first
strand. Sequences are labelled by species name (Mm--Mus
musculus, Hs--Homo sapiens, Gg--Gallus gallus, Xl--Xenopus
laevis, Dm--Drosophila melanogaster, Dv--Drosophila virilis,
Os--Oryza sativa, Zm--Zea mays, At--Arabidopsis thaliana,
Dc--Daucus carota, Sp--Schizosaccharomyces pombe,
Ec--Encephalitozoon cuniculi, Ce--Caenorhabditis elegans,
Le--Lycopersicon esculentum).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
489-499)
copyright 2004.
).
Residues important for recognition of the PXVXL motif are
highlighted in yellow (Val-224) and red (Pro-222/Leu-226 at the
-2/+2 positions). Residues that form the hydrophobic patch that
interacts with the flanking N- and C-terminal sequences
(Phe-217/Ile-218 and Ile-229/Leu-230 at the -6/-7 and +5/+6
positions, respectively) are highlighted in blue. Residues that
are not conserved and are predicted to alter specificity are
boxed. Conserved residues that define the fold of the shadow
domain are highlighted in grey, while residues important for
dimerisation are indicated by blue triangles. Phe-163 (indicated
by a green dot) is important for both the structure of the
shadow domain and peptide binding. The positions of secondary
structure elements in mouse HP1 
-helices)--the
dots indicate the positions of the conserved bulges in the first
strand. Sequences are labelled by species name (Mm--Mus
musculus, Hs--Homo sapiens, Gg--Gallus gallus, Xl--Xenopus
laevis, Dm--Drosophila melanogaster, Dv--Drosophila virilis,
Os--Oryza sativa, Zm--Zea mays, At--Arabidopsis thaliana,
Dc--Daucus carota, Sp--Schizosaccharomyces pombe,
Ec--Encephalitozoon cuniculi, Ce--Caenorhabditis elegans,
Le--Lycopersicon esculentum).