Abstract
The X-ray structure of the uncomplexed human chimeric Fab′ of the anti-tumor antibody BR96 has been determined at 2.6 Å resolution. The structure has been compared with Lewis Y antigen-complexed structures of BR96 which were determined previously. The comparison reveals segmental motions and/or conformational rearrangements of three CDR loops (L1, L3, and H2), whereas CDR H3 does not undergo changes upon complexation despite its significant main-chain contacts to the carbo hydrate antigen. In light of the uncomplexed chimeric Fab′ structure reported here, the previously observed high mobility of the CL:CH1 domains of the complexed chimeric BR96 Fab is rationalized as a “swinging” motion approximately about the axis of the elbow bend.
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