2e4u: Difference between revisions

Revision as of 02:16, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2e4u.png

Template:STRUCTURE 2e4u

Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with L-glutamateCrystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with L-glutamate

Template:ABSTRACT PUBMED 17360426

About this StructureAbout this Structure

2E4U is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Mon Jul 28 02:16:55 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2e4u.gif|left|200px]]
+{{Seed}}
+[[Image:2e4u.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2e4u|  PDB=2e4u  |  SCENE=  }}
-'''Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with L-glutamate'''
+===Crystal structure of the extracellular region of the group II metabotropic glutamate receptor complexed with L-glutamate===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17360426}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17360426 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17360426}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: G-protein-coupled receptor]]
 [[Category: Neuron]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:55:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:16:55 2008''