Figure 1.
Figure 1. Structure of the dystrophin - -dystroglycan
complex. a, Ribbon diagram showing the overall organization
of the dystroglycan binding region of dystrophin. The WW domain
is colored yellow, the first EF-hand domain green, the second
EF-hand domain blue, and additional helices gold. The -dystroglycan
peptide (white) extends across the first EF-hand and the WW
domain. Elements of secondary structure, the N- and C-termini of
the protein, and peptide are labeled. b, Molecular surface of
the DBR, colored as in (a). The surface of residues in the WW
domain and EF-hand that contact the peptide are shaded bright
yellow and dark green, respectively, to highlight the binding
surface. Peptide residues Pro 889 -Tyr 892 constitute the PPxY
motif. All Pro residues in the peptide are in the trans
conformation; those in the PPxY motif form a single turn of
polyproline II helix. c , Detailed view of dystrophin - -dystroglycan
recognition. The thin red lines indicate hydrogen bonds. The
peptide makes six hydrogen bonds directly to the DBR domain, and
an additional six through bridging water molecules (indicated by
red spheres).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2000,
7,
634-638)
copyright 2000.
-dystroglycan
complex. a, Ribbon diagram showing the overall organization
of the dystroglycan binding region of dystrophin. The WW domain
is colored yellow, the first EF-hand domain green, the second
EF-hand domain blue, and additional helices gold. The 
-dystroglycan
peptide (white) extends across the first EF-hand and the WW
domain. Elements of secondary structure, the N- and C-termini of
the protein, and peptide are labeled. b, Molecular surface of
the DBR, colored as in (a). The surface of residues in the WW
domain and EF-hand that contact the peptide are shaded bright
yellow and dark green, respectively, to highlight the binding
surface. Peptide residues Pro 889 -Tyr 892 constitute the PPxY
motif. All Pro residues in the peptide are in the trans
conformation; those in the PPxY motif form a single turn of
polyproline II helix. c , Detailed view of dystrophin -