Figure 1.
FIG. 1. Stereoview of the crystal structure of
rhFXI[370-607]-ecotinM84R. A, a C trace of
rhFXI[370-607]-ecotinM84R tetramer. The ecotinM84R molecules are
colored in blue and yellow, and the rhFXI[370-607] molecules are
colored in green and red. The N and C termini of each molecule
are labeled in the same color as the molecule. The primary and
secondary binding sites between rhFXI[370-607] and ecotinM84R
are indicated by arrows. B, a ribbon diagram of the catalytic
domain of FXIa in the rhFXI[370-607]-ecotinM84R crystal
structure. The helices are colored in
purple and sheets are in green. A
few key residues, discussed in the text, are presented in a
ball-and-stick representation with CPK coloring. The N and C
termini are indicated. All figures were prepared with DINO
(www.dino3.org) and Povray (www.povray.org).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
4704-4712)
copyright 2005.
trace of
rhFXI[370-607]-ecotinM84R tetramer. The ecotinM84R molecules are
colored in blue and yellow, and the rhFXI[370-607] molecules are
colored in green and red. The N and C termini of each molecule
are labeled in the same color as the molecule. The primary and
secondary binding sites between rhFXI[370-607] and ecotinM84R
are indicated by arrows. B, a ribbon diagram of the catalytic
domain of FXIa in the rhFXI[370-607]-ecotinM84R crystal
structure. The 
sheets are in green. A
few key residues, discussed in the text, are presented in a
ball-and-stick representation with CPK coloring. The N and C
termini are indicated. All figures were prepared with DINO
(www.dino3.org) and Povray (www.povray.org).