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Figure 2.
Figure 2. Overall Structure of the Complex between the
Aggrecan CLD and FnIII Repeats 3–5 of Tenascin-R, TN3–5
A consistent coloring scheme is used throughout for the
different domains. Surfaces, cartoon elements, and carbon atoms
from domain 3 are colored beige, those in domain 4 are colored
cyan, and those in domain 5 are purple. Figure 2, Figure 3,
Figure 4 and Figure 7 were made using Pymol
(http://www.pymol.org).
(A) Secondary structure cartoon.
The three Ca^2+ ions are shown as yellow spheres. The boxes
marked a–c denote the interaction areas for which detailed
views are given in Figures 4A–4C.
(B) Surface
representation colored by domain.
(C) Exploded “open
book” view of the interaction surface. The aggrecan CLD has
been rotated 90° around a horizontal axis in the plane of
the paper, TN3–5 in the opposite direction. The cyan and
purple patches on the surface of the CLD represent the
interaction areas with TN4 and TN5, respectively. Similarly, the
maroon patches on the surface of TN3–5 represent the
interaction area with the CLD.
(D) The aggrecan CLD amino
acid residues mediating interaction with tenascin-R form a
surface corresponding to the sulfopeptide binding surface of
P-selectin in complex with PSGL-1 (Somers et al., 2000). The
interaction surface of P-selectin with the protein part of the
PSGL-1 sulfoglycopeptide on is colored cyan, and the
carbohydrate interaction surface is colored purple. The part of
the PSGL-1 peptide visible in the crystal structure is shown as
a ball-and-stick model. The figure is in the same orientation as
the lower part of Figure 2C, showing the interaction surface of
tenascin-R on aggrecan.
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