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Figure 4.
Figure 4. Structure of the sB7-1 Homodimer Observed in the
Crystal Lattice(A) Two orthogonal views of the GRASP surface of
the homodimer showing the location of residues whose mutation to
alanine disrupts (magenta) or has no effect (cyan) on binding.
Putative N-glycosylation sites are colored green.(B) The GRASP
surfaces of amino acids involved in forming the dimer are
colored red. The view is identical to the right-hand panel in
(A) but with the front copy of sB7-1 removed.(C) Details of the
residues at the dimer interface are shown in ball-and-stick
format viewed as in the left-hand panel of (A).(D) The homodimer
is shown with either oligomannose, bi-, or triantennary
N-glycans modeled at each of the potential glycosylation sites.
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