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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
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BMC Structural Biology

ISSN: 1472-6807

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