2e4v: Difference between revisions

New page: left|200px<br /><applet load="2e4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e4v, resolution 2.4Å" /> '''Crystal structure of ...
 
No edit summary
Line 1: Line 1:
[[Image:2e4v.gif|left|200px]]<br /><applet load="2e4v" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2e4v.gif|left|200px]]<br /><applet load="2e4v" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2e4v, resolution 2.4&Aring;" />
caption="2e4v, resolution 2.4&Aring;" />
'''Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV'''<br />
'''Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with DCG-IV'''<br />


==Overview==
==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.
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==
2E4V 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 NAG and 2CG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E4V OCA].  
2E4V 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=NAG:'>NAG</scene> and <scene name='pdbligand=2CG:'>2CG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4V OCA].  


==Reference==
==Reference==
Line 23: Line 23:
[[Category: neuron]]
[[Category: neuron]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:56:51 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:00 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA