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PDBsum entry 3o28
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Transport protein
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PDB id
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3o28
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transport protein
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Title:
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Ligand-binding domain of glua2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
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Structure:
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Glutamate receptor 2. Chain: a. Fragment: ligand binding domain, unp residues 413 to 527 and 653 to 796. Synonym: glur-2, glur-b, glur-k2, glutamate receptor ionotropic, ampa 2, glua2, ampa-selective glutamate receptor 2. Engineered: yes. Other_details: s1-s2 fusion in which gly118 and thr119 replace a membrane-spanning region
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: gria2, glur2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.00Å
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R-factor:
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0.184
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R-free:
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0.234
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Authors:
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J.K.F.Maclean,S.Basten,R.A.Campbell,I.A.Cumming,K.J.Gillen, J.Gillespie,C.Jamieson,B.Kazemier,M.Kiczun,Y.Lamont,A.J.Lyons, E.M.Moir,J.A.Morrow,M.Papakosta,Z.Rankovic,L.Smith
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Key ref:
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C.Jamieson
et al.
(2010).
A novel series of positive modulators of the AMPA receptor: discovery and structure based hit-to-lead studies.
Bioorg Med Chem Lett,
20,
5753-5756.
PubMed id:
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Date:
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22-Jul-10
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Release date:
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15-Sep-10
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PROCHECK
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Headers
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References
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P19491
(GRIA2_RAT) -
Glutamate receptor 2 from Rattus norvegicus
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Seq:
Struc:
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883 a.a.
260 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 6 residue positions (black
crosses)
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Bioorg Med Chem Lett
20:5753-5756
(2010)
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PubMed id:
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A novel series of positive modulators of the AMPA receptor: discovery and structure based hit-to-lead studies.
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C.Jamieson,
S.Basten,
R.A.Campbell,
I.A.Cumming,
K.J.Gillen,
J.Gillespie,
B.Kazemier,
M.Kiczun,
Y.Lamont,
A.J.Lyons,
J.K.Maclean,
E.M.Moir,
J.A.Morrow,
M.Papakosta,
Z.Rankovic,
L.Smith.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.L.Mayer
(2011).
Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.
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Curr Opin Neurobiol,
21,
283-290.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
