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Structure paper

TitleSubunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers
Journal, issue, pagesEmbo J., Vol. 30, Page 959-971, Year 2011
Publish dateJun 11, 2009 (structure data deposition date)
AuthorsRossmann, M. / Sukumaran, M. / Penn, A.C. / Veprintsev, D.B. / Babu, M.M. / Greger, I.H.
External linksEmbo J. / PubMed:21317873
MethodsX-ray diffraction
Resolution1.75 - 3.2 Å
Structure data

PDB-3hsy:
High resolution structure of a dimeric GluR2 N-terminal domain (NTD)
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-3n6v:
Structure of the GluA2 NTD-dimer interface mutant, T78A
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-3o2j:
Structure of the GluA2 NTD-dimer interface mutant, N54A
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / GLUTAMATE RECEPTOR / LIGAND-GATED ION CHANNEL / SYNAPSE / CELL JUNCTION / CELL MEMBRANE / ENDOPLASMIC RETICULUM / GLYCOPROTEIN / ION TRANSPORT / IONIC CHANNEL / LIPOPROTEIN / MEMBRANE / PALMITATE / PHOSPHOPROTEIN / POSTSYNAPTIC CELL MEMBRANE / RECEPTOR / RNA EDITING / TRANSMEMBRANE / TRANSPORT / AMPA / assembly / NTD / GluR2 / GluA2 / periplasmatic binding protein / ATD / Oligomerization

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