2e4z
From Proteopedia
(New page: 200px<br /><applet load="2e4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e4z, resolution 3.30Å" /> '''Crystal structure of...) |
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| - | [[Image:2e4z.jpg|left|200px]]<br /><applet load="2e4z" size=" | + | [[Image:2e4z.jpg|left|200px]]<br /><applet load="2e4z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2e4z, resolution 3.30Å" /> | caption="2e4z, resolution 3.30Å" /> | ||
'''Crystal structure of the ligand-binding region of the group III metabotropic glutamate receptor'''<br /> | '''Crystal structure of the ligand-binding region of the group III metabotropic glutamate receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Metabotropic glutamate receptors play major roles in the activation of | + | Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements. |
==About this Structure== | ==About this Structure== | ||
| - | 2E4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2E4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: neuron]] | [[Category: neuron]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:02 2008'' |
Revision as of 15:06, 21 February 2008
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Crystal structure of the ligand-binding region of the group III metabotropic glutamate receptor
Overview
Metabotropic glutamate receptors play major roles in the activation of excitatory synapses in the central nerve system. We determined the crystal structure of the entire extracellular region of the group II receptor and that of the ligand-binding region of the group III receptor. A comparison among groups I, II, and III provides the structural basis that could account for the discrimination of group-specific agonists. Furthermore, the structure of group II includes the cysteine-rich domain, which is tightly linked to the ligand-binding domain by a disulfide bridge, suggesting a potential role in transmitting a ligand-induced conformational change into the downstream transmembrane region. The structure also reveals the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of the dimeric receptors on the cell surface. We propose a general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements.
About this Structure
2E4Z is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors., Muto T, Tsuchiya D, Morikawa K, Jingami H, Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):3759-64. Epub 2007 Feb 26. PMID:17360426
Page seeded by OCA on Thu Feb 21 17:06:02 2008
