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Proposed orientation of antigen/antibody complex of monomeric human lipoprotein lipase (hLPL) and an FAb fragment of an hLPL-specific monoclonal antibody (MAb) 5D2 when bound to a C-terminal epitope. The proposed 3D-structure of hLPL and the FAb of an MAb with similar epitope specificity as 5D2 are based on those reported by Tilbeurgh et al. (1994. J. Biol. Chem. 269: 4626-4633), and Ghiara et al. (1994. Science. 264: 82-85), respectively. Indicated are: amino acids of the active site of hLPL, the lid covering its active center, potential heparin binding regions, a dodecamer of heparin and the possible orientation towards hLPL, as well as the side chains of hLPL amino acids that are probably in direct contact with the binding site of hLPL-specific MAb 5D2. (See Chang, et al., p. 2350.)
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