Figure 1.
(a) Schematic domain organization of the HHIP receptor. SP,
signal peptide; L1 and L2, interdomain linker regions; EGF1 and
EGF2, epidermal growth factor repeat domains; Hx,
membrane-attachment helix. -propeller
blades are color coded and numbered. Proteolytic cleavage site
residues Arg189 and Arg210, identified by N-terminal sequencing,
are highlighted. The crystallization construct (eHHIP N)
and the stabilized full-length ectodomain construct (eHHIPS) are
shown. (b) SeMet SAD-phased and phase-extended electron density
map (calculated to 2.8 Å, contoured at 1 )
with a rainbow-colored C trace
of eHHIP N.
(c) Ribbon diagram of eHHIP N
with color coding as in a and b. The six blades of the -propeller
domain (each consisting of a four-stranded -sheet)
are numbered as in a. The 11 disulfide bridges are shown in
black stick representation and marked with Roman numerals. (d)
Electrostatic properties. eHHIP N
is shown as solvent-accessible surface colored by electrostatic
potential contoured at 10
kT (red, acidic; blue, basic). The prominent negatively charged
patch that interacts with Hh ligands is marked with a dotted
circle.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Nat Struct Biol
(2009,
16,
698-703)
copyright 2009.
-propeller
blades are color coded and numbered. Proteolytic cleavage site
residues Arg189 and Arg210, identified by N-terminal sequencing,
are highlighted. The crystallization construct (eHHIP 
N)
and the stabilized full-length ectodomain construct (eHHIPS) are
shown. (b) SeMet SAD-phased and phase-extended electron density
map (calculated to 2.8 Å, contoured at 1 
)
with a rainbow-colored C 
trace
of eHHIP 
10
kT (red, acidic; blue, basic). The prominent negatively charged
patch that interacts with Hh ligands is marked with a dotted
circle.