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PDB: 7 results

7MEU
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BU of 7meu by Molmil
A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders
Descriptor: (2E)-2-{2-[4-([1,1'-biphenyl]-4-yl)-1,3-thiazol-2-yl]hydrazinylidene}-3-(2-nitrophenyl)propanoic acid, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE, Eukaryotic translation initiation factor 4E
Authors:Papadopoulos, E.
Deposit date:2021-04-07
Release date:2021-04-28
Last modified:2023-10-18
Method:X-RAY DIFFRACTION (1.91 Å)
Cite:A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders.
Eur.J.Med.Chem., 219, 2021
1Z65
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BU of 1z65 by Molmil
Mouse Doppel 1-30 peptide
Descriptor: Prion-like protein doppel
Authors:Papadopoulos, E.
Deposit date:2005-03-21
Release date:2006-02-07
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:NMR Solution Structure of the Peptide Fragment 1-30, Derived from Unprocessed Mouse Doppel Protein, in DHPC Micelles
Biochemistry, 45, 2006
2KZ8
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BU of 2kz8 by Molmil
Solution NMR structure of MqsA, a protein from E. coli, containing a Zinc finger, N-terminal and a Helix Turn-Helix C-terminal domain
Descriptor: Uncharacterized HTH-type transcriptional regulator ygiT
Authors:Papadopoulos, E, Vlamis-Gardikas, A, Graslund, A, Billeter, M, Holmgren, A, Collet, J.
Deposit date:2010-06-14
Release date:2011-06-29
Last modified:2024-05-01
Method:SOLUTION NMR
Cite:Solution structure and biophysical properties of MqsA, a Zn-containing antitoxin from Escherichia coli
Biochim.Biophys.Acta, 2012
4TQC
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BU of 4tqc by Molmil
The co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G
Descriptor: (2S)-3-(4-amino-3-nitrophenyl)-2-{2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinyl}propanoic acid, 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE, Eukaryotic translation initiation factor 4E
Authors:Papadopoulos, E, Jenni, S, Wagner, G.
Deposit date:2014-06-10
Release date:2014-08-13
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G.
Proc.Natl.Acad.Sci.USA, 111, 2014
4TPW
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BU of 4tpw by Molmil
The co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G
Descriptor: (2E)-2-{2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene}-3-(2-nitrophenyl)propanoic acid, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE, ...
Authors:Papadopoulos, E, Jenni, S, Wagner, G.
Deposit date:2014-06-09
Release date:2014-08-13
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G.
Proc.Natl.Acad.Sci.USA, 111, 2014
4TQB
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BU of 4tqb by Molmil
The co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G
Descriptor: (2E)-2-{2-[4-(4-bromophenyl)-1,3-thiazol-2-yl]hydrazinylidene}-3-(2-nitrophenyl)propanoic acid, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE, ...
Authors:Papadopoulos, E, Jenni, S, Wagner, G.
Deposit date:2014-06-10
Release date:2014-08-13
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.59 Å)
Cite:Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G.
Proc.Natl.Acad.Sci.USA, 111, 2014
2K44
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BU of 2k44 by Molmil
Solution structure of a K+-channel voltage-sensor paddle domain
Descriptor: K+-channel voltage-sensor paddle domain of Calcium-activated potassium channel subunit alpha-1
Authors:Unnerstale, S, Lind, J, Papadopoulos, E, Maler, L.
Deposit date:2008-05-28
Release date:2009-06-02
Last modified:2024-05-29
Method:SOLUTION NMR
Cite:Solution structure of the HsapBK K+-channel voltage-sensor paddle sequence
Biochemistry, 2009

226707

數據於2024-10-30公開中

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