We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2v3t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v3t.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2v3t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v3t| PDB=2v3t | SCENE= }}
{{STRUCTURE_2v3t| PDB=2v3t | SCENE= }}
-
'''STRUCTURE OF THE LIGAND-BINDING CORE OF THE IONOTROPIC GLUTAMATE RECEPTOR-LIKE GLURDELTA2 IN THE APO FORM'''
+
===STRUCTURE OF THE LIGAND-BINDING CORE OF THE IONOTROPIC GLUTAMATE RECEPTOR-LIKE GLURDELTA2 IN THE APO FORM===
-
==Overview==
+
<!--
-
The orphan glutamate-like receptor GluRdelta2 is predominantly expressed in Purkinje cells of the central nervous system. The classification of GluRdelta2 to the ionotropic glutamate receptor family is based on sequence similarities, because GluRdelta2 does not form functional homomeric glutamate-gated ion channels in transfected cells. Studies in GluRdelta2(-/-) knockout mice as well as in mice with naturally occurring mutations in the GluRdelta2 gene have demonstrated an essential role of GluRdelta2 in cerebellar long-term depression, motor learning, motor coordination, and synaptogenesis. However, the lack of a known agonist has hampered investigations on the function of GluRdelta2. In this study, the ligand-binding core of GluRdelta2 (GluRdelta2-S1S2) was found to bind neutral amino acids such as D-serine and glycine, as demonstrated by isothermal titration calorimetry. Direct evidence for binding of D-serine and structural rearrangements in the binding cleft of GluRdelta2-S1S2 is provided by x-ray structures of GluRdelta2-S1S2 in its apo form and in complex with D-serine. Functionally, D-serine and glycine were shown to inactivate spontaneous ion-channel conductance in GluRdelta2 containing the lurcher mutation (EC(50) values, 182 and 507 microM, respectively). These data demonstrate that the GluRdelta2 ligand-binding core is capable of binding ligands and that cleft closure of the ligand-binding core can induce conformational changes that alter ion permeation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17715062}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17715062 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17715062}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:09:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:19:33 2008''

Revision as of 11:19, 27 July 2008

Image:2v3t.png

Template:STRUCTURE 2v3t

STRUCTURE OF THE LIGAND-BINDING CORE OF THE IONOTROPIC GLUTAMATE RECEPTOR-LIKE GLURDELTA2 IN THE APO FORM

Template:ABSTRACT PUBMED 17715062

About this Structure

2V3T is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Ionotropic glutamate-like receptor delta2 binds D-serine and glycine., Naur P, Hansen KB, Kristensen AS, Dravid SM, Pickering DS, Olsen L, Vestergaard B, Egebjerg J, Gajhede M, Traynelis SF, Kastrup JS, Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):14116-21. Epub 2007 Aug 21. PMID:17715062

Page seeded by OCA on Sun Jul 27 14:19:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v3t"
Personal tools