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Structure paper

TitleMolecular mechanism of flop selectivity and subsite recognition for an AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in complexes with PEPA.
Journal, issue, pagesBiochemistry, Vol. 49, Page 2843-2850, Year 2010
Publish dateMar 9, 2010 (structure data deposition date)
AuthorsAhmed, A.H. / Ptak, C.P. / Oswald, R.E.
External linksBiochemistry / PubMed:20199107
MethodsX-ray diffraction
Resolution1.793 - 2.5 Å
Structure data

PDB-3m3f:
PEPA bound to the ligand binding domain of GluA3 (flop form)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3m3k:
Ligand binding domain (S1S2) of GluA3 (flop)
Method: X-RAY DIFFRACTION / Resolution: 1.793 Å

PDB-3m3l:
PEPA bound to the ligand binding domain of GluA2 (flop form)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-P99:
2-[2,6-difluoro-4-({2-[(phenylsulfonyl)amino]ethyl}sulfanyl)phenoxy]acetamide

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / glutamate receptor / GluA3 / GluR3 / AMPA receptor / neurotransmitter receptor / S1S2 / GluR2 / GluA2 / allosteric modulator

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