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Document Table 3 Residues Involved in ADP Binding in Glycosomal and Human PGK T.brucei Human_1 a Human_2 b In contact with ADP moiety Ala 242 Gly 238 Gly 238 Adenine Tyr 245 Phe 241 Tyr 241 Adenine Lys 259 Leu 256 Leu 256 Adenine Ala 314 Gly 309 Gly 309 Adenine Ser 378 Thr 375 Thr 375 β-phosphate a Somatic PGK [67]. b PGK in spermatogenic cells [68]. Page 377 commercially available. However, its sequence has been determined [67] and appears to be 97% identical to horse and pig PGK. For completeness it should be mentioned that there is a second human PGK in testis tissue that is 87% identical to the somatic enzyme [68]. The crystal structures of the apo-enzyme from horse [31] and of the binary complex between pig PGK and its substrate [32] (Figure 8) are available from the Protein Databank. The substrate was found to bind to the N-terminal domain of the enzyme. The binding site for ADP is known from the structure of its binary complex with PGK from B. stearothermophilus [69]. It resides in the Cterminal domain. Since the substrate and ADP binding sites are 10 Å apart, a hinge-bending motion between the two domains has been postulated to occur during catalysis [70]. Kinetically glycosomal PGK from T. brucei and mammalian PGK are very similar: the K m values for ATP are 0.29 and 0.46 and mM, respectively; the K m values for 3-phosphoglycerate are 1.62 and 0.62 mM, respectively (due to the unavailability of the human enzyme the rabbit muscle enzyme was used as a substitute) [71]. The residues responsible for binding the substrate [32] are identical between human and glycosomal PGK [72]. However, five of the residues involved in the binding of ADP differ between the two enzymes (Table 3). Apparently, the biggest difference between human PGK and the parasite enzyme is the charged residue Lys259, which has the apolar Leu256 as a human counterpart. Molecules that bind at the ADP binding site and specifically recognize Lys259 might therefore be good starting points for drug design. III. Search For New Leads A. Triosephosphate Isomerase: The Crystallographic Cocktail Soak Approach http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_377.html (1 of 2) [4/5/2004 5:39:43 PM]
Document Because there are no known leads that bind to the selectivity region of TIM, the design of selective inhibitors is an exercise in de novo ligand design. We tried to http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_377.html (2 of 2) [4/5/2004 5:39:43 PM]
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Document D ddI, 152 tumour necrosis
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Document [Protease targets] serinyl
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