About the Cover
Cover: Three-dimensional homology models for human pigment epithelium-derived factor (PEDF). They were created using computer-assisted molecular modeling based on the X-ray crystal structure of the uncleaved form of antithrombin III (an inhibitory, heparin-binding serpin) as described in Biochemistry. 1998;37: 10643-10652. (Top Left) Backbone tracing (gray) of the PEDF model with a cluster of basic residue side chains shown in ball-and-stick representations (blue) forming the putative glycosaminoglycan binding region. (Bottom right) Opposite side view of the model to the top left with a region spanning between PEDF positions 78-121 shown in green that contains a neurotrophic active site and receptor binding region (J Biol Chem 1999;274:31605-31612).(Center) Rotation of the above molecules about 90° reveals that the glycosaminoglycan-binding region and the neutrophic active site, are two distinct and nonoverlapping areas of the PEDF protein and both away from the homologous serpin reactive site, P1. Other features of the model are labeled: "N" and "C" for amino- and carboxy-termini.
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