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Figure 2.
FIGURE 2. The NMR structure of Tcad1. Tcad1 adopts as the
other characterized cadherin domains a β-barrel structure (A)
with a Greek key folding topology (B). Open boxes mark residues
with a β-bulge conformation. As Tcad1 is monomeric in the
presence and absence of calcium, residues Ile-2-Val-3 and
Val-25-Asp-26 can participate in a stable β-sheet structure
(pink colored strands). The pairing of the strands is
antiparallel except for the parallel arrangement of strands B
and I. A stereoview of the superposition of the 20 final in a
water shell refined structures is shown in C. The β-strands are
colored as in A and B. Glycines with positive  -angles
are depicted in yellow and prolines that adopt a cis-peptide
bond conformation in red. All structure pictures were made with
the programs MolMol (49) and POV-Ray.
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