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Table 3 Residues involved with MTA binding to the three MTAPs

From: Leishmania infantum 5’-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target

huMTAP T18a P69b A94a C95b G96b F177 I194b N195b M196 T197a T219 D220 D222 V231b V233 V236
Li MTAP G16 G17 R60 H61 H65 P69 I92 N93 A94 F181 G199 M200 T201 M221 M243 V247
Tb MTAP G18 H62 H66 V93 N94 A95 M204 A225 M247 N250 V251 V254
MEME motifs 5 5 2 2 2 2 3 3 3 3 3 1 1 1 1 1 1 1 1 1 4 4 4 4
  1. The table illustrates interacting residues (IRs) with MTA at a distance lower than or equal to a cutoff of 4Ǻ. Residues listed in the same column are structurally aligned IRs. As we did not dock the cofactor on the proteins, it was expected not to observe interactions on huMTAP involving the cofactor binding sites (R60, H61, T93). However, three cofactor- binding sites (a) were here identified as IR with MTA. (b) Corresponds to residues here identified as IRs but not on the crystal structure of huMTAP