56. Stockman BJ, Nirmala NR, Wagner G, Delcamp TJ, DeYarman MT, Freishman JH
(1991)
Methotrexate
binds
in
a
non-productive orientation to human dihydrofolate reductase in solution, based on
NMR spectroscopy. FEBS Lett 283
(2):267–269
57. Oefner C, D’Arcy A, Winkler FK (1988)
Crystal structure of human DHFR complexed
with folate. Eur J Biochem 174:377–385
58. Huang FY, Yang QX, Huang T (1991) 15N
NMR studies of the conformation of E. coli
DHFR in complex with folate or methotrexate. FEBS Lett 289(2):231–234
59. Cheung HT, Birdsall B, Feeny J (1992)
13CNMR studies of complexes of Ecoli
DHFR formed with methotrexate and with
folic acid. FEBS Lett 312(2):147–151
60. Curtis N, Moore S, Birdsall B, Bloxsidge J,
Gibson CL, Jones JR, Feeny J (1994)
3H-NMR studies of multiple conformations
and dynamic processes in complexes of folate
and methotrexate with L. casei DHFR. Biochem J 303:401–405
61. Bolin JT, Filman DJ, Matthews DA, Hamlin
RC, Kraut J (1982) Crystal structures of E
coli and Lactobacillus casei DHFR refined at
1.7A resolution: general features and binding
of methotrexate. J Biol Chem 257
(22):13650–13662
62. Kielhofner MA (1990) Trimethoprim-sulfamethoxazole-pharmacokinetics, clinical uses,
and adverse reactions. Tex Heart Inst J 17
(2):87–93
63. Baker DJ, Beddell CR, Champness JN, Goodford PJ, Norrington FEA, Smith DR, Stammers DK (1981) The binding of
trimethoprim to bacterial dihydrofolate
reductase. FEBS Lett 126(1):49–52
64. Kovalevskaya NV, Smurnyi ED, Birdsall B,
Feeney J, Polshavoc VI (2007) Structural factors determining the binding selectivity of the
antibacterial drug trimethoprim to dihydrofolate reductase. Pharm Chem J 41(7):350–353
65. Lemke TL, Roche VF, Williams DA, Zito SW
(2013) Foye’s principles of medicinal chemistry, 7th edn. Lippincott Williams & Wilkins, a
Wolters Kluwer business, Baltimore
66. Feeney J, Birdsall B, Kovalevskaya NV, Smurnyy YD, Navarro Peran EM, Polshakov VI
(2011) NMR structures of apo L. casei dihydrofolate reductase and its complexes with
trimethoprim and NADPH: contributions to
positive cooperative binding from ligandinduced refolding, conformational changes,
and interligand hydrophobic interactions.
Biochemistry 50(18):3609–3620
67. Kovalevskaya NV, Smurnyy YD, Polshakov
VI, Birdsall B, Bradbury AF, Frenkiel T, Feeney J (2005) Solution structure of human
dihydrofolate reductase in its complex with
trimethoprim and NADPH. J Biomol NMR
33(1):69–72
68. Champness JNS (1986) D.K.; Beddell, C.R.,
crystallographic investigation of the cooperative interaction between trimethoprim,
reduced cofactor and dihydrofolate reductase.
FEBS Lett 199(1):61–67
69. Polshakov VI, Smirnov EG, Birdsall B,
Kelly G, Feeney J (2002) Letter to the editor:
NMR-based solution structure of the complex of lactobacillus casei DHFR with trimethoprim and NADPH. J Biomol NMR
24:67–70
70. Huang F, Yang Q, Huang T, Gelbaum L,
Kuyper LF (1991) The conformations of trimethoprim/E. coli dihydrofolate reductase
complexes: A 15N and 31P NMR study.
FEBS Lett 283(1):44–46
71. Birdsall B, Bevan AW, Pascaul C, Roberts
GCK, Feeny J, Gronenborn A, Clore GM
(1984) Multinuclear NMR characterization
of two coexisting conformational states of
the Lactobacillus casei DHFR-trimethoprimNADP+
complex.
Biochemistry
23:4733–4742
72. Gronenborn A, Birdsall B, Hyde E, Roberts
GCK, Feeney J, Burgen ASV (1981) Direct
observation by NMR of two coexisting conformations of an enzyme ligand complex in
solution. Nature 290:273–274
73. Gronenborn A, Birdsall B, Hyde E,
Roberts G, Feeney J, Burgen A (1981) 1H
and 31P NMR characterization of two conformations of the trimethoprim-NADP+
DHFR complex. Mol Pharmacol 20:145–153
74. Kongsaeree
P,
Khongsuk
P,
Leartsakulpanich
U,
Chitnumsub
P,
Tarnchompoo B, Walkinshaw MD, Yuthavong Y (2005) Crystal structure of dihydrofolate reductase from plasmodium vivaxpyrimethamine displacement linked with
mutation-induced resistance. Proc Natl Acad
Sci U S A 102(37):13046–13051
75. Volpato JP, Pelletier JN (2009) Mutational
‘hot-spots’ in mammalian, bacterial and protozoal dihydrofolate reductases associated
with antifolate resistance: sequence and structural comparison. Drug Resist Updat 12
(1–2):28–41
Distal Regions Regulate Dihydrofolate Reductase-Ligand Interactions
217
(1991)
Methotrexate
binds
in
a
non-productive orientation to human dihydrofolate reductase in solution, based on
NMR spectroscopy. FEBS Lett 283
(2):267–269
57. Oefner C, D’Arcy A, Winkler FK (1988)
Crystal structure of human DHFR complexed
with folate. Eur J Biochem 174:377–385
58. Huang FY, Yang QX, Huang T (1991) 15N
NMR studies of the conformation of E. coli
DHFR in complex with folate or methotrexate. FEBS Lett 289(2):231–234
59. Cheung HT, Birdsall B, Feeny J (1992)
13CNMR studies of complexes of Ecoli
DHFR formed with methotrexate and with
folic acid. FEBS Lett 312(2):147–151
60. Curtis N, Moore S, Birdsall B, Bloxsidge J,
Gibson CL, Jones JR, Feeny J (1994)
3H-NMR studies of multiple conformations
and dynamic processes in complexes of folate
and methotrexate with L. casei DHFR. Biochem J 303:401–405
61. Bolin JT, Filman DJ, Matthews DA, Hamlin
RC, Kraut J (1982) Crystal structures of E
coli and Lactobacillus casei DHFR refined at
1.7A resolution: general features and binding
of methotrexate. J Biol Chem 257
(22):13650–13662
62. Kielhofner MA (1990) Trimethoprim-sulfamethoxazole-pharmacokinetics, clinical uses,
and adverse reactions. Tex Heart Inst J 17
(2):87–93
63. Baker DJ, Beddell CR, Champness JN, Goodford PJ, Norrington FEA, Smith DR, Stammers DK (1981) The binding of
trimethoprim to bacterial dihydrofolate
reductase. FEBS Lett 126(1):49–52
64. Kovalevskaya NV, Smurnyi ED, Birdsall B,
Feeney J, Polshavoc VI (2007) Structural factors determining the binding selectivity of the
antibacterial drug trimethoprim to dihydrofolate reductase. Pharm Chem J 41(7):350–353
65. Lemke TL, Roche VF, Williams DA, Zito SW
(2013) Foye’s principles of medicinal chemistry, 7th edn. Lippincott Williams & Wilkins, a
Wolters Kluwer business, Baltimore
66. Feeney J, Birdsall B, Kovalevskaya NV, Smurnyy YD, Navarro Peran EM, Polshakov VI
(2011) NMR structures of apo L. casei dihydrofolate reductase and its complexes with
trimethoprim and NADPH: contributions to
positive cooperative binding from ligandinduced refolding, conformational changes,
and interligand hydrophobic interactions.
Biochemistry 50(18):3609–3620
67. Kovalevskaya NV, Smurnyy YD, Polshakov
VI, Birdsall B, Bradbury AF, Frenkiel T, Feeney J (2005) Solution structure of human
dihydrofolate reductase in its complex with
trimethoprim and NADPH. J Biomol NMR
33(1):69–72
68. Champness JNS (1986) D.K.; Beddell, C.R.,
crystallographic investigation of the cooperative interaction between trimethoprim,
reduced cofactor and dihydrofolate reductase.
FEBS Lett 199(1):61–67
69. Polshakov VI, Smirnov EG, Birdsall B,
Kelly G, Feeney J (2002) Letter to the editor:
NMR-based solution structure of the complex of lactobacillus casei DHFR with trimethoprim and NADPH. J Biomol NMR
24:67–70
70. Huang F, Yang Q, Huang T, Gelbaum L,
Kuyper LF (1991) The conformations of trimethoprim/E. coli dihydrofolate reductase
complexes: A 15N and 31P NMR study.
FEBS Lett 283(1):44–46
71. Birdsall B, Bevan AW, Pascaul C, Roberts
GCK, Feeny J, Gronenborn A, Clore GM
(1984) Multinuclear NMR characterization
of two coexisting conformational states of
the Lactobacillus casei DHFR-trimethoprimNADP+
complex.
Biochemistry
23:4733–4742
72. Gronenborn A, Birdsall B, Hyde E, Roberts
GCK, Feeney J, Burgen ASV (1981) Direct
observation by NMR of two coexisting conformations of an enzyme ligand complex in
solution. Nature 290:273–274
73. Gronenborn A, Birdsall B, Hyde E,
Roberts G, Feeney J, Burgen A (1981) 1H
and 31P NMR characterization of two conformations of the trimethoprim-NADP+
DHFR complex. Mol Pharmacol 20:145–153
74. Kongsaeree
P,
Khongsuk
P,
Leartsakulpanich
U,
Chitnumsub
P,
Tarnchompoo B, Walkinshaw MD, Yuthavong Y (2005) Crystal structure of dihydrofolate reductase from plasmodium vivaxpyrimethamine displacement linked with
mutation-induced resistance. Proc Natl Acad
Sci U S A 102(37):13046–13051
75. Volpato JP, Pelletier JN (2009) Mutational
‘hot-spots’ in mammalian, bacterial and protozoal dihydrofolate reductases associated
with antifolate resistance: sequence and structural comparison. Drug Resist Updat 12
(1–2):28–41
Distal Regions Regulate Dihydrofolate Reductase-Ligand Interactions
217