2v3t: Difference between revisions

Revision as of 14:19, 27 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:2v3t.png

Template:STRUCTURE 2v3t

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

Template:ABSTRACT PUBMED 17715062

About this StructureAbout this Structure

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

ReferenceReference

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

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OCA

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-'''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
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+{{ABSTRACT_PUBMED_17715062}}
 ==About this Structure==
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 [[Category: Transmembrane]]
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