This component provides a mechanism for obtaining details structural information concerning how high-affinity peptide and RNA ligands generated by Selectide and SELEX technologies bind to their target proteins. Specifically, we propose to crystallize various HIV encoded proteins with the most potent peptide and oligonucleotide ligands that emerge from screening extensive libraries of randomized peptide and RNA sequences. These co-crystals will then be used in x-ray diffraction studies to provide a structural basis for the elaboration of these novel initial lead molecules into important therapeutic agents for the treatment of AIDS.
