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Figure 5.
Figure 5 Comparison of the CDR3s of the Sea and Mcg Bence-Jones
dimers, presented as stereo diagrams. Components of monomer B
(H-chain analogs) are colored magenta and segments of monomer A
(L chains) are yellow. CDR3 loops act as pillars of the active
sites and their relative locations in each dimer largely
determine the magnitudes of the openings into the binding
cavities. This opening is significantly narrower in the Sea
dimer (8 versus 15 Å), but the depths are practically the same.
The phenylalanine residues at the lower ends mark the floors of
the cavities. This figure was prepared with the program
MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst.
24, 946-950.]).
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