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Structure paper

TitleEnhancing Action of Positive Allosteric Modulators through the Design of Dimeric Compounds.
Journal, issue, pagesJ. Med. Chem., Vol. 61, Page 5279-5291, Year 2018
Publish dateDec 18, 2017 (structure data deposition date)
AuthorsDrapier, T. / Geubelle, P. / Bouckaert, C. / Nielsen, L. / Laulumaa, S. / Goffin, E. / Dilly, S. / Francotte, P. / Hanson, J. / Pochet, L. ...Drapier, T. / Geubelle, P. / Bouckaert, C. / Nielsen, L. / Laulumaa, S. / Goffin, E. / Dilly, S. / Francotte, P. / Hanson, J. / Pochet, L. / Kastrup, J.S. / Pirotte, B.
External linksJ. Med. Chem. / PubMed:29775064
MethodsX-ray diffraction
Resolution1.4 Å
Structure data

PDB-6faz:
Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the positive allosteric modulator TDPAM01 at 1.4 A resolution.
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-D45:
6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide)

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / AMPA receptor / GluA2 / Ligand-binding Domain / GluA2-S1S2J / positive allosteric modulator

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