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PDBsum entry 4xoy
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PDB id:
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Transferase
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Title:
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Crystal structure of erk2 in complex with an inhibitor
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Structure:
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Mitogen-activated protein kinase 1. Chain: a. Fragment: unp residues 8-358. Synonym: mapk 1,ert1,extracellular signal-regulated kinase 2,erk-2, map kinase isoform p42,p42-mapk,mitogen-activated protein kinase 2, mapk 2. Engineered: yes
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: mapk1, erk2, mapk, prkm1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.10Å
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R-factor:
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0.183
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R-free:
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0.219
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Authors:
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M.Gelin,F.Allemand,G.Labesse,J.F.Guichou
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Key ref:
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M.Gelin
et al.
(2015).
Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.
Acta Crystallogr D Biol Crystallogr,
71,
1777-1787.
PubMed id:
DOI:
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Date:
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16-Jan-15
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Release date:
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12-Aug-15
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PROCHECK
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Headers
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References
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P63086
(MK01_RAT) -
Mitogen-activated protein kinase 1 from Rattus norvegicus
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Seq:
Struc:
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358 a.a.
330 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.11.24
- mitogen-activated protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:1777-1787
(2015)
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PubMed id:
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Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.
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M.Gelin,
V.Delfosse,
F.Allemand,
F.Hoh,
Y.Sallaz-Damaz,
M.Pirocchi,
W.Bourguet,
J.L.Ferrer,
G.Labesse,
J.F.Guichou.
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ABSTRACT
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X-ray crystallography is an established technique for ligand screening in
fragment-based drug-design projects, but the required manual handling steps -
soaking crystals with ligand and the subsequent harvesting - are tedious and
limit the throughput of the process. Here, an alternative approach is reported:
crystallization plates are pre-coated with potential binders prior to protein
crystallization and X-ray diffraction is performed directly `in situ' (or
in-plate). Its performance is demonstrated on distinct and relevant therapeutic
targets currently being studied for ligand screening by X-ray crystallography
using either a bending-magnet beamline or a rotating-anode generator. The
possibility of using DMSO stock solutions of the ligands to be coated opens up a
route to screening most chemical libraries.
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