Figure 5.
Figure 5 Features of the Nrp VEGF- and heparin-binding domains.
(A) The molecular surface of the rat (PDB code 2ORZ) (Vander
Kooi et al, 2007) and human b1b2 crystal structures are colored
as described in Figure 4D. Green arrows indicate an acidic
groove that is formed by the 'spikes' in the b1 domain
(Supplementary Figure S5); this feature forms the
Tuftsin-binding site of rat Nrp1. Yellow arrows indicate the
approximate location of the heparin-binding patch. (B) The
sequence conservation (green, 100%; yellow, than
or equal to 75%) of the b1b2 domains among 12 Nrps
(Supplementary Figure S3) was mapped onto the surface of the
human Nrp1 b1b2 structure. Two highly conserved patches are
delineated in red. Residues outlined in cyan indicate those
residues that contact the Fab in the anti-Nrp1^B-Fab/b1 complex.
The a2 domain (tan) is shown by using a superposition of the
b1b2 and a2b1b2 structures from Nrp1. (C) Ribbon representation
of the anti-Nrp1^B–Fab/b1 complex (yellow, b1; orange, heavy
chain; gray, light chain). (D) The anti-Nrp1^B/b1 interface. The
b1 domain is depicted as a molecular surface with a green arrow
indicating the Tuftsin/VEGF tail-binding groove. Only CDRs H3
and L1 contact b1.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
EMBO J
(2007,
26,
4902-4912)
copyright 2007.
than
or equal to 75%) of the b1b2 domains among 12 Nrps
(Supplementary Figure S3) was mapped onto the surface of the
human Nrp1 b1b2 structure. Two highly conserved patches are
delineated in red. Residues outlined in cyan indicate those
residues that contact the Fab in the anti-Nrp1^B-Fab/b1 complex.
The a2 domain (tan) is shown by using a superposition of the
b1b2 and a2b1b2 structures from Nrp1. (C) Ribbon representation
of the anti-Nrp1^B–Fab/b1 complex (yellow, b1; orange, heavy
chain; gray, light chain). (D) The anti-Nrp1^B/b1 interface. The
b1 domain is depicted as a molecular surface with a green arrow
indicating the Tuftsin/VEGF tail-binding groove. Only CDRs H3
and L1 contact b1.