This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1p1e

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:23, 8 September 2021

Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins

Structural highlights

1p1e is a 1 chain structure with sequence from Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1p1d
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GRIP1_RAT] May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The interaction of the glutamate receptor subunits 2 and 3 (GluR2/3) with multi-PDZ domain glutamate receptor-interacting protein (GRIP) is important for the synaptic trafficking and clustering of the receptors. Binding of GluR2/3 to GRIP requires both the fourth and fifth PDZ domains (PDZ4 and PDZ5) to be covalently linked, although only one PDZ domain is directly involved in binding to the receptor tail. To elucidate the molecular basis of this mode of PDZ domain-mediated target recognition, we solved the solution structures of the PDZ45 tandem and the isolated PDZ4 of GRIP. The two PDZ domains form a compact structure with a fixed interdomain orientation. The interdomain packing and the stable folding of both PDZ domains require a short stretch of amino acids N-terminal to PDZ4 and a conserved linker connecting PDZ4 and PDZ5. PDZ4 contains a deformed aB-bB groove that is unlikely to bind to carboxyl peptides. Instead, the domain stabilizes the structure of PDZ5.

Tandem PDZ repeats in glutamate receptor-interacting proteins have a novel mode of PDZ domain-mediated target binding.,Feng W, Shi Y, Li M, Zhang M Nat Struct Biol. 2003 Nov;10(11):972-8. Epub 2003 Oct 12. PMID:14555997^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dong H, O'Brien RJ, Fung ET, Lanahan AA, Worley PF, Huganir RL. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature. 1997 Mar 20;386(6622):279-84. PMID:9069286 doi:http://dx.doi.org/10.1038/386279a0
↑ Feng W, Shi Y, Li M, Zhang M. Tandem PDZ repeats in glutamate receptor-interacting proteins have a novel mode of PDZ domain-mediated target binding. Nat Struct Biol. 2003 Nov;10(11):972-8. Epub 2003 Oct 12. PMID:14555997 doi:10.1038/nsb992

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p1e"

@@ Line 3: / Line 3: @@
 <StructureSection load='1p1e' size='340' side='right'caption='[[1p1e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1p1e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P1E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1p1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P1E FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p1d|1p1d]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p1d|1p1d]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p1e OCA], [http://pdbe.org/1p1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p1e RCSB], [http://www.ebi.ac.uk/pdbsum/1p1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p1e ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p1e OCA], [https://pdbe.org/1p1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p1e RCSB], [https://www.ebi.ac.uk/pdbsum/1p1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p1e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GRIP1_RAT GRIP1_RAT]] May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons.<ref>PMID:9069286</ref>
+[[https://www.uniprot.org/uniprot/GRIP1_RAT GRIP1_RAT]] May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons.<ref>PMID:9069286</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1p1e

From Proteopedia

Revision as of 09:23, 8 September 2021

Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox