3en3: Difference between revisions
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{{STRUCTURE_3en3| PDB=3en3 | SCENE= }} | {{STRUCTURE_3en3| PDB=3en3 | SCENE= }} | ||
===Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate=== | ===Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate=== | ||
{{ABSTRACT_PUBMED_19102704}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/GRIA4_RAT GRIA4_RAT]] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).<ref>PMID:12603841</ref> <ref>PMID:19102704</ref> <ref>PMID:20107073</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[3en3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[3en3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EN3 OCA]. | ||
==See Also== | ==See Also== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:019102704</ref><references group="xtra"/> | <ref group="xtra">PMID:019102704</ref><references group="xtra"/><references/> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Gill, A.]] | [[Category: Gill, A.]] | ||
[[Category: Madden, D R.]] | [[Category: Madden, D R.]] | ||
Revision as of 07:44, 2 April 2014
Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate
Template:ABSTRACT PUBMED 19102704
Function
[GRIA4_RAT] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).[1] [2] [3]
About this Structure
3en3 is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA.
See Also
Reference
- Gill A, Birdsey-Benson A, Jones BL, Henderson LP, Madden DR. Correlating AMPA receptor activation and cleft closure across subunits: crystal structures of the GluR4 ligand-binding domain in complex with full and partial agonists. Biochemistry. 2008 Dec 30;47(52):13831-41. PMID:19102704 doi:10.1021/bi8013196
- ↑ Pasternack A, Coleman SK, Fethiere J, Madden DR, LeCaer JP, Rossier J, Pasternack M, Keinanen K. Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain. J Neurochem. 2003 Mar;84(5):1184-92. PMID:12603841
- ↑ Gill A, Birdsey-Benson A, Jones BL, Henderson LP, Madden DR. Correlating AMPA receptor activation and cleft closure across subunits: crystal structures of the GluR4 ligand-binding domain in complex with full and partial agonists. Biochemistry. 2008 Dec 30;47(52):13831-41. PMID:19102704 doi:10.1021/bi8013196
- ↑ Birdsey-Benson A, Gill A, Henderson LP, Madden DR. Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors. J Neurosci. 2010 Jan 27;30(4):1463-70. PMID:20107073 doi:30/4/1463
