Figure 1.
Fig. 1. Overall topology of the GPIb N-terminal
domain. Ribbon diagram of the topology viewed from the side and
a 90° rotated view facing the concave surface of the
leucine-rich repeats are shown. The three short 3[10] helices
are colored light blue, and the helix in
the C-terminal flank is colored dark blue. Convex face -strands are
colored green, and concave face -strands are
colored gray. Five expressed BSS mutations, which cause loss of
vWF binding, are shown as black balls. L57F and C65R localize to
LRR2 with L129P, A156V, and L179del localized to the LRR5, LRR6,
and LRR7 -strands
respectively. The regulatory (R)-loop is colored orange with
activating platelet-type von Willebrand disease mutations G233V
and M239V indicated as orange balls. The anionic region is
colored red with the molecular structure of the sulfated
tyrosine residues 276, 278, and 279 shown in full.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
35657-35663)
copyright 2002.
N-terminal
domain. Ribbon diagram of the topology viewed from the side and
a 90° rotated view facing the concave surface of the
leucine-rich repeats are shown. The three short 3[10] helices
are colored light blue, and the 
-strands are
colored green, and concave face