2i3v
From Proteopedia
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[[Image:2i3v.png|left|200px]] | [[Image:2i3v.png|left|200px]] | ||
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{{STRUCTURE_2i3v| PDB=2i3v | SCENE= }} | {{STRUCTURE_2i3v| PDB=2i3v | SCENE= }} | ||
===Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant=== | ===Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant=== | ||
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{{ABSTRACT_PUBMED_17018279}} | {{ABSTRACT_PUBMED_17018279}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2i3v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3V OCA]. | + | [[2i3v]] is a 4 chain structure of [[Ionotropic Glutamate Receptors]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3V OCA]. |
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| + | ==See Also== | ||
| + | *[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:017018279</ref><ref group="xtra">PMID:009865957</ref><references group="xtra"/> |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Armstrong, N.]] | [[Category: Armstrong, N.]] | ||
Revision as of 06:49, 27 July 2012
Contents |
Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant
Template:ABSTRACT PUBMED 17018279
About this Structure
2i3v is a 4 chain structure of Ionotropic Glutamate Receptors with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E. Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell. 2006 Oct 6;127(1):85-97. PMID:17018279 doi:10.1016/j.cell.2006.08.037
- Chen GQ, Sun Y, Jin R, Gouaux E. Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct. Protein Sci. 1998 Dec;7(12):2623-30. PMID:9865957
