Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovis

Begley, D.W.; Edwards, T.E.; Raymond, A.C.; Smith, E.R.; Hartley, R.C.; Abendroth, J.; Sankaran, B.; Lorimer, D.D.; Myler, P.J.; Staker, B.L.; Stewart, L.J.

doi:10.1107/S1744309111029009

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Substrates and cofactors of dihydrofolate reductase (DHFR) [dihydrofolate (DHF) and nicotinamide adenine dinucleotide phosphate (NADP), respectively] and thymidylate synthase (TS) [5′-deoxyuridine monophosphate (dUMP) and N⁵,N¹⁰-methylene-5,6,7,8-tetrahydrofolate (mTHF), respectively]. Also shown are the two folate analogs and TS inhibitors raltitrexed (RTX) and pemetrexed (PTX).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1070-1077

doi:10.1107/S1744309111029009

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