2egn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2egn.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2egn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2egn| PDB=2egn | SCENE= }}
{{STRUCTURE_2egn| PDB=2egn | SCENE= }}
-
'''Crystal Structure of Tamalin PDZ Domain in Complex with mGluR5 C-terminal Peptide'''
+
===Crystal Structure of Tamalin PDZ Domain in Complex with mGluR5 C-terminal Peptide===
-
==Overview==
+
<!--
-
Metabotropic glutamate receptors (mGluRs) function as neuronal G-protein-coupled receptors and this requires efficient membrane targeting through associations with cytoplasmic proteins. However, the molecular mechanism regulating mGluR cell-surface trafficking remains unknown. We report here that mGluR trafficking is controlled by the autoregulatory assembly of a scaffold protein Tamalin. In the absence of mGluR, Tamalin self-assembles into autoinhibited conformations, through its PDZ domain and C-terminal intrinsic ligand motif. X-ray crystallographic analyses visualized integral parts of the oligomeric self-assemblies of Tamalin, which require not only the novel hydrophobic dimerization interface but also canonical and noncanonical PDZ/ligand autoinhibitory interactions. The mGluR cytoplasmic region can competitively bind to Tamalin at a higher concentration, disrupting weak inhibitory interactions. The atomic view of mGluR association suggests that this rearrangement is dominated by electrostatic attraction and repulsion. We also observed in mammalian cells that the association liberates the intrinsic ligand toward a motor protein receptor, thereby facilitating mGluR cell-surface trafficking. Our study suggests a novel regulatory mechanism of the PDZ domain, by which Tamalin switches between the trafficking-inhibited and -active forms depending on mGluR association.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17396155}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17396155 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17396155}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Pdz domain]]
[[Category: Pdz domain]]
[[Category: Peptide complex]]
[[Category: Peptide complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:31:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:21:51 2008''

Revision as of 06:21, 28 July 2008

Image:2egn.png

Template:STRUCTURE 2egn

Crystal Structure of Tamalin PDZ Domain in Complex with mGluR5 C-terminal Peptide

Template:ABSTRACT PUBMED 17396155

About this Structure

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

Reference

Crystal structures of autoinhibitory PDZ domain of Tamalin: implications for metabotropic glutamate receptor trafficking regulation., Sugi T, Oyama T, Muto T, Nakanishi S, Morikawa K, Jingami H, EMBO J. 2007 Apr 18;26(8):2192-205. Epub 2007 Mar 29. PMID:17396155

Page seeded by OCA on Mon Jul 28 09:21:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2egn"
Personal tools