Figure 2.
FIGURE 2. Docked structure of dp10 heparin in complex with
TSPN-1. A, TSPN-1·dp10 low energy complex identified
using AutoDock4. TSPN-1 residues involved in the hydrogen
bonding network are rendered in ball-and-stick. Each residue
involved in the hydrogen bonding network is annotated. For
clarity hydrogen bonds are not displayed. Each domain is labeled
and rendered as a ribbon drawing, with -helices colored green
(domain A) or magenta (domain B), and β-strands and random coil
are colored cyan (domain A) or yellow (domain B). The heparin
moiety dp10 is rendered in ball and stick representation. B,
Molcad surface of the TSPN-1·dp10 complex with residues
involved in the hydrogen bonding network colored in blue. This
view of the TSPN-1·dp10 complex is the result of rotating
the complex –90° around the x-axis (out of the plane of
the page or screen) to provide a view of this complex from the
heparin binding site, which is located at the base of complex in
panel A. Figs. 2B and 4B were prepared using the SYBYL suite of
programs (Tripos).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
283,
3932-3941)
copyright 2007.
-helices colored green
(domain A) or magenta (domain B), and β-strands and random coil
are colored cyan (domain A) or yellow (domain B). The heparin
moiety dp10 is rendered in ball and stick representation. B,
Molcad surface of the TSPN-1·dp10 complex with residues
involved in the hydrogen bonding network colored in blue. This
view of the TSPN-1·dp10 complex is the result of rotating
the complex –90° around the x-axis (out of the plane of
the page or screen) to provide a view of this complex from the
heparin binding site, which is located at the base of complex in
panel A. Figs. 2B and 4B were prepared using the SYBYL suite of
programs (Tripos).