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Figure 1.
Figure 1. Schematic Representation of the Structure of the
NF-kB Dimerization Domains(A) The wild-type homodimeric
conformation and (B) the intertwined fold of the MLAM mutant are
shown. The mutations are Tyr267->Met and Val310->Met. Two loops
in the MLAM mutant that could not be built into the structure
due to disorder are labeled (residues from 285 to 290 in both
chains). The extensive intertwining between the two polypeptide
chains is responsible for excluding from the solvent a total
surface area of about 4600 Å2. Orthogonal views are shown.
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