Figure 3.
Fig. 3. Main chain schematic of the vWF-A1 domain, with
-strands
(arrows) and helices (coils) (drawn with MOLSCRIPT, RASTER3D,
and RENDER (32-34)). The two cysteines involved the disulfide
bridge are shown as yellow spheres. Sites of von Willebrand
disease type IIb mutations (both natural and induced) are shown
as red spheres. Mutants with reduced botrocetin binding are in
green. Mutations with selective loss-of-function (reduced
ristocetin-induced binding but normal botrocetin-induced
binding) are in cyan (23) or black (26), and a mutant with
reduced GpIb binding but normal botrocetin binding is in blue
(23). The mutation of KKKK642-645 in the 5- E loop also
reduces binding to heparin (26). For multiple site mutants,
spheres are placed near the midpoint of the mutation.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
10396-10401)
copyright 1998.
-strands
(arrows) and helices (coils) (drawn with MOLSCRIPT, RASTER3D,
and RENDER (32-34)). The two cysteines involved the disulfide
bridge are shown as yellow spheres. Sites of von Willebrand
disease type IIb mutations (both natural and induced) are shown
as red spheres. Mutants with reduced botrocetin binding are in
green. Mutations with selective loss-of-function (reduced
ristocetin-induced binding but normal botrocetin-induced
binding) are in cyan (23) or black (26), and a mutant with
reduced GpIb binding but normal botrocetin binding is in blue
(23). The mutation of KKKK642-645 in the 
5-