Figure 1.
Figure 1: Sequence homology and structure of Arfaptin. a,
Sequence homology between five Arfaptin homologues. The -helical
elements derived from the crystal structure are indicated and
coloured as in b. The N terminus of the Arfaptin fragment used
in this study, which encompasses the entire predicted
coiled-coil region of these molecules, is indicated by the black
triangle. Residues absolutely conserved between the six Arfaptin
homologues are indicated by blue circles. b, Three orthogonal
views of the Arfaptin dimer in ribbons representation26. Top,
Arfaptin dimer viewed along its dyad axis. Helices A, B and C of
each monomer are red, green and blue, respectively, and the
dimer-related helices are labelled A', B' and C'. Middle,
Arfaptin dimer viewed along the long axis, illustrating the
cavity created by the five-helix barrel at the dimer interface.
Bottom, Arfaptin viewed with its long axis horizontal and the
dyad axis vertical, showing the crescent-like shape of the dimer.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2001,
411,
215-219)
copyright 2001.
-helical
elements derived from the crystal structure are indicated and
coloured as in b. The N terminus of the Arfaptin fragment used
in this study, which encompasses the entire predicted
coiled-coil region of these molecules, is indicated by the black
triangle. Residues absolutely conserved between the six Arfaptin
homologues are indicated by blue circles. b, Three orthogonal
views of the Arfaptin dimer in ribbons representation26. Top,
Arfaptin dimer viewed along its dyad axis. Helices A, B and C of
each monomer are red, green and blue, respectively, and the
dimer-related helices are labelled A', B' and C'. Middle,
Arfaptin dimer viewed along the long axis, illustrating the
cavity created by the five-helix barrel at the dimer interface.
Bottom, Arfaptin viewed with its long axis horizontal and the
dyad axis vertical, showing the crescent-like shape of the dimer.