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Figure 2.
Fi. 2. A: Model structure of he extracellular domain of gp39.
The structureofthehomotrimer is in green. The y-axis
is approximately to thethreefold molecular symmetry
axis. he locations f site-specific natural gp39 mutants in three
patients (C.D., A.Y. and J.W.) are These mutations im-
pair thefunction of gp39 in these patients.One of thethree
symmetry-related region n gp39 that correspond o the receptor-
binding sites in tumor necrosis factor beta (TNFP) is in
Locations of the three mutations shown heresuggests that
residue changes may interfere with the binding ofgp39 to
receptor CD40. B: Comparison of calculated 3D-profiles,
a 21-residue window, forthe trimeric tumor necrosis fac-
orapha (TNFa) crystal andthe trimeric gp39 model structure
elative to their sequences. The calculated Z-scores the TNFa
structure and sequence and forthe gp39 model and se-
were 30.8 and 32.8,respectively. The analysis supports
he proposed structral similarity of gp39 and
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