Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T35940 | Target Info | |||
| Target Name | ERK activator kinase 1 (MEK1) | ||||
| Synonyms | PRKMK1; Mitogen-activated protein kinase kinase 1; MKK1; MEK 1; MAPKK 1; MAPK/ERKkinase 1; MAPK/ERK kinase 1; MAP kinase kinase 1; Dual specificity mitogen-activated protein kinase kinase 1 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | MAP2K1 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Adenosine triphosphate | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N | ||||
| InChI | 1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1 | ||||
| InChIKey | ZKHQWZAMYRWXGA-KQYNXXCUSA-N | ||||
| PubChem Compound ID | 5957 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3VVH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 TRSYMSPERL235 QGTHYSVQSD245 IWSMGLSLVE255 MAVGRYPIPP265 PDAKELELMF 275 PPMAIFELLD315 YIVNEPPPKL325 PSGVFSLEFQ335 DFVNKCLIKN345 PAERADLKQL 355 MVHAFIKRSD365 AEEVDFAGWL375 CSTIGLN
|
|||||
|
|
LEU74
3.829
GLY75
3.665
ALA76
3.605
GLY77
3.208
ASN78
2.732
GLY79
4.522
GLY80
3.890
VAL81
4.739
VAL82
3.551
ALA95
3.433
LYS97
2.766
VAL127
4.280
MET143
3.330
|
|||||
| PDB ID: 1S9J X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [2] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 VGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPPMAIFEL313 LDYIVNEPPP323 KLPSGVFSLE333 FQDFVNKCLI343 KNPAERADLK 353 QLMVHAFIKR363 SDAEEVDFAG373 WLCSTIGLN
|
|||||
|
|
LEU74
4.072
GLY75
3.811
ALA76
3.623
GLY77
2.684
ASN78
3.115
GLY80
3.678
VAL82
3.582
ALA95
3.444
LYS97
2.600
VAL127
4.427
MET143
3.383
GLU144
2.968
|
|||||
| PDB ID: 3E8N X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) complexed with a potent inhibitor RDEA119 and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [3] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 NSVGTRSYMS231 PERLQGTHYS241 VQSDIWSMGL251 SLVEMAVGRY261 PIPPPDAKEL 271 ELMFPPMAIF311 ELLDYIVNEP321 PPKLPSGVFS331 LEFQDFVNKC341 LIKNPAERAD 351 LKQLMVHAFI361 KRSDAEEVDF371 AGWLCSTIGL381 N
|
|||||
|
|
LEU74
3.770
GLY75
4.016
ALA76
3.910
GLY77
3.665
ASN78
3.403
GLY79
4.109
GLY80
3.452
VAL81
4.800
VAL82
3.075
ALA95
3.448
LYS97
2.894
VAL127
4.388
MET143
3.217
GLU144
2.880
|
|||||
| PDB ID: 3DY7 X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [4] |
| PDB Sequence |
ELKDDDFEKI
71 SELGAGNGGV81 VFKVSHKPSG91 LVMARKLIHL101 EIKPAIRNQI111 IRELQVLHEC 121 NSPYIVGFYG131 AFYSDGEISI141 CMEHMDGGSL151 DQVLKKAGRI161 PEQILGKVSI 171 AVIKGLTYLR181 EKHKIMHRDV191 KPSNILVNSR201 GEIKLCDFGV211 SGQLIDSMAN 221 GTRSYMSPER234 LQGTHYSVQS244 DIWSMGLSLV254 EMAVGRYPIP264 PPPMAIFELL 314 DYIVNEPPPK324 LPSGVFSLEF334 QDFVNKCLIK344 NPAERADLKQ354 LMVHAFIKRS 364
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.663
GLY75
3.649
ALA76
4.067
GLY77
3.419
ASN78
3.392
GLY80
3.593
VAL81
4.632
VAL82
4.136
ALA95
3.553
LYS97
2.679
VAL127
4.271
MET143
3.298
GLU144
2.841
|
|||||
| PDB ID: 3V04 Discovery of Novel Allosteric MEK Inhibitors Possessing Classical and Non-classical Bidentate Ser212 Interactions. | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [5] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 VGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPPMAIFEL313 LDYIVNEPPP323 KLPSGVFSLE333 FQDFVNKCLI343 KNPAERADLK 353 QLMVHAFIKR363 SDAEEVDFAG373 WLCSTIGLN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:208; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.856
GLY75
4.033
ALA76
3.577
GLY77
2.550
ASN78
3.571
GLY80
3.465
VAL81
4.956
VAL82
3.528
ALA95
3.430
LYS97
2.533
VAL127
4.550
MET143
3.568
GLU144
3.040
|
|||||
| PDB ID: 3V01 Discovery of Novel Allosteric MEK Inhibitors Possessing Classical and Non-classical Bidentate Ser212 Interactions. | ||||||
| Method | X-ray diffraction | Resolution | 2.71 Å | Mutation | No | [5] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 VGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPPMAIFEL313 LDYIVNEPPP323 KLPSGVFSLE333 FQDFVNKCLI343 KNPAERADLK 353 QLMVHAFIKR363 SDAEEVDFAG373 WLCSTIGLN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.962
GLY75
4.051
ALA76
3.358
GLY77
2.898
ASN78
3.269
GLY80
3.350
VAL82
3.394
ALA95
3.452
LYS97
2.581
VAL127
4.507
MET143
3.596
GLU144
2.897
HIS145
3.924
|
|||||
| PDB ID: 3EQB X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.62 Å | Mutation | No | [6] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 VGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPPMAIFEL313 LDYIVNEPPP323 KLPSGVFSLE333 FQDFVNKCLI343 KNPAERADLK 353 QLMVHAFIKR363 SDAEEVDFAG373 WLCSTIGLN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.690
GLY75
3.845
ALA76
3.777
GLY77
2.581
ASN78
4.347
GLY80
3.825
VAL81
3.932
VAL82
3.703
ALA95
3.466
LYS97
2.433
VAL127
4.292
MET143
3.276
GLU144
2.862
|
|||||
| PDB ID: 2P55 X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [7] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 VGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPPMAIFEL313 LDYIVNEPPP323 KLPSGVFSLE333 FQDFVNKCLI343 KNPAERADLK 353 QLMVHAFIKR363 SDAEEVDFAG373 WLCSTIGLN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:147 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:208; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.094
GLY75
3.008
ALA76
3.040
GLY77
2.989
ASN78
3.679
GLY80
3.431
VAL81
4.719
VAL82
2.891
ALA95
3.475
LYS97
2.508
VAL127
3.957
MET143
2.855
GLU144
1.909
|
|||||
| PDB ID: 3PP1 Crystal Structure of the Human Mitogen-activated protein kinase kinase 1 (MEK 1) in complex with ligand and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [8] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 NSFVGTRSYM230 SPERLQGTHY240 SVQSDIWSMG250 LSLVEMAVGR260 YPIPPPDAKE 270 LELMFPMAIF311 ELLDYIVNEP321 PPKLPSGVFS331 LEFQDFVNKC341 LIKNPAERAD 351 LKQLMVHAFI361 KRSDAEEVDF371 AGWLCSTIGL381 N
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208 or .A:224; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.818
GLY75
3.737
ALA76
3.722
GLY77
2.807
ASN78
2.719
GLY80
3.387
VAL81
4.722
VAL82
3.841
ALA95
3.536
LYS97
2.667
VAL127
4.226
MET143
3.386
GLU144
2.922
HIS145
3.964
|
|||||
| PDB ID: 3DV3 MEK1 with PF-04622664 Bound | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [4] |
| PDB Sequence |
MELKDDDFEK
70 ISELGAGNGG80 VVFKVSHKPS90 GLVMARKLIH100 LEIKPAIRNQ110 IIRELQVLHE 120 CNSPYIVGFY130 GAFYSDGEIS140 ICMEHMDGGS150 LDQVLKKAGR160 IPEQILGKVS 170 IAVIKGLTYL180 REKHKIMHRD190 VKPSNILVNS200 RGEIKLCDFG210 VSGQLIDSMA 220 NGTRSYMSPE233 RLQGTHYSVQ243 SDIWSMGLSL253 VEMAVGRYPI263 PPPDAKELEL 273 MFPMAIFELL314 DYIVNEPPPK324 LPSGVFSLEF334 QDFVNKCLIK344 NPAERADLKQ 354 LMVHAFIKRS364 DAEEVDFAGW374 LCSTIGLN
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:208; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.889
GLY75
3.912
ALA76
3.676
GLY77
3.309
ASN78
2.821
GLY80
3.648
VAL81
4.840
VAL82
3.515
ALA95
3.378
LYS97
2.785
VAL127
4.248
MET143
3.279
GLU144
2.943
|
|||||
| PDB ID: 3OS3 Mitogen-activated protein kinase kinase 1 (MEK1) in complex with CH4858061 and MgATP | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [9] |
| PDB Sequence |
ELKDDDFEKI
71 SELGAGNGGV81 VFKVSHKPSG91 LVMARKLIHL101 EIKPAIRNQI111 IRELQVLHEC 121 NSPYIVGFYG131 AFYSDGEISI141 CMEHMDGGSL151 DQVLKKAGRI161 PEQILGKVSI 171 AVIKGLTYLR181 EKHKIMHRDV191 KPSNILVNSR201 GEIKLCDFGV211 SGQLIDSMAN 221 SFVGTRSYMS231 PERLQGTHYS241 VQSDIWSMGL251 SLVEMAVGRY261 PIPMAIFELL 314 DYIVNEPPPK324 LPVFSLEFQD336 FVNKCLIKNP346 AERADLKQLM356 VHAFIKRSDA 366 EEVDFAGWLC376 ST
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:147 or .A:149 or .A:150 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.499
GLY75
3.438
ALA76
2.998
GLY77
3.480
ASN78
2.962
GLY80
4.014
VAL81
4.095
VAL82
2.966
ALA95
3.490
LYS97
2.942
VAL127
4.198
MET143
3.566
GLU144
2.679
|
|||||
| PDB ID: 4AN3 Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [10] |
| PDB Sequence |
MALGELKDDD
67 FEKISELGAG77 NGGVVFKVSH87 KPSGLVMARK97 LIHLEIKPAI107 RNQIIRELQV 117 LHECNSPYIV127 GFYGAFYSDG137 EISICMEHMD147 GGSLDQVLKK157 AGRIPEQILG 167 KVSIAVIKGL177 TYLREKHKIM187 HRDVKPSNIL197 VNSRGEIKLC207 DFGVSGQLID 217 EMANEGTRSY229 MSPERLQGTH239 YSVQSDIWSM249 GLSLVEMAVG259 RYPRPPMAIF 311 ELLDYIVNEP321 PPKLPSAVFS331 LEFQDFVNKC341 LIKNPAERAD351 LKQLMVHAFI 361 KRSDAEEVDF371 AGWLCSTIGL381
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:79 or .A:80 or .A:81 or .A:82 or .A:95 or .A:97 or .A:127 or .A:143 or .A:144 or .A:145 or .A:146 or .A:149 or .A:150 or .A:152 or .A:153 or .A:190 or .A:192 or .A:194 or .A:195 or .A:197 or .A:207 or .A:208 or .A:226; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU74
3.124
GLY75
4.081
ALA76
3.970
GLY77
3.522
ASN78
2.839
GLY79
4.379
GLY80
3.505
VAL81
4.982
VAL82
3.687
ALA95
3.388
LYS97
2.642
VAL127
3.986
MET143
3.417
GLU144
2.938
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor and MgATP | ||||
| REF 2 | Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol. 2004 Dec;11(12):1192-7. | ||||
| REF 3 | RDEA119/BAY 869766: a potent, selective, allosteric inhibitor of MEK1/2 for the treatment of cancer.Cancer Res.2009 Sep 1;69(17):6839-47. | ||||
| REF 4 | Beyond the MEK-pocket: can current MEK kinase inhibitors be utilized to synthesize novel type III NCKIs? Does the MEK-pocket exist in kinases other than MEK?. Bioorg Med Chem Lett. 2009 Jan 1;19(1):226-9. | ||||
| REF 5 | Discovery of novel allosteric mitogen-activated protein kinase kinase (MEK) 1,2 inhibitors possessing bidentate Ser212 interactions. J Med Chem. 2012 May 24;55(10):4594-604. | ||||
| REF 6 | 2-Alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles-O-Alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK (MAP ERK kinase). Bioorg Med Chem Lett. 2008 Dec 1;18(23):6171-4. | ||||
| REF 7 | 4-anilino-5-carboxamido-2-pyridone derivatives as noncompetitive inhibitors of mitogen-activated protein kinase kinase. J Med Chem. 2007 Oct 18;50(21):5090-102. | ||||
| REF 8 | Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer. Bioorg Med Chem Lett. 2011 Mar 1;21(5):1315-9. | ||||
| REF 9 | Design and synthesis of novel allosteric MEK inhibitor CH4987655 as an orally available anticancer agent. Bioorg Med Chem Lett. 2011 Mar 15;21(6):1795-801. | ||||
| REF 10 | Novel Carboxamide-Based Allosteric MEK Inhibitors: Discovery and Optimization Efforts toward XL518 (GDC-0973). ACS Med Chem Lett. 2012 Apr 9;3(5):416-21. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.