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2fcf

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Revision as of 07:14, 24 February 2021

The crystal structure of the 7th PDZ domain of MPDZ (MUPP-1)

Structural highlights

2fcf is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	MPDZ, MUPP1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MPDZ_HUMAN] Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses.^[1] ^[2]

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

PDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions.

Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.,Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233^[3]

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

References

↑ Becamel C, Figge A, Poliak S, Dumuis A, Peles E, Bockaert J, Lubbert H, Ullmer C. Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1. J Biol Chem. 2001 Apr 20;276(16):12974-82. Epub 2001 Jan 9. PMID:11150294 doi:http://dx.doi.org/10.1074/jbc.M008089200
↑ Krapivinsky G, Medina I, Krapivinsky L, Gapon S, Clapham DE. SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation. Neuron. 2004 Aug 19;43(4):563-74. PMID:15312654 doi:10.1016/j.neuron.2004.08.003
↑ Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA. Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions. Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233 doi:16/4/683

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/2fcf"

@@ Line 1: / Line 1: @@
 ==The crystal structure of the 7th PDZ domain of MPDZ (MUPP-1)==
-<StructureSection load='2fcf' size='340' side='right' caption='[[2fcf]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+<StructureSection load='2fcf' size='340' side='right'caption='[[2fcf]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fcf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FCF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fcf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCF FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MPDZ, MUPP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MPDZ, MUPP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2fcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcf OCA], [http://pdbe.org/2fcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fcf RCSB], [http://www.ebi.ac.uk/pdbsum/2fcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fcf 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=2fcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcf OCA], [https://pdbe.org/2fcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fcf RCSB], [https://www.ebi.ac.uk/pdbsum/2fcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fcf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MPDZ_HUMAN MPDZ_HUMAN]] Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses.<ref>PMID:11150294</ref> <ref>PMID:15312654</ref>
+[[https://www.uniprot.org/uniprot/MPDZ_HUMAN MPDZ_HUMAN]] Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses.<ref>PMID:11150294</ref> <ref>PMID:15312654</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Arrowsmith, C]]
 [[Category: Berridge, G]]

2fcf

From Proteopedia

Revision as of 07:14, 24 February 2021

The crystal structure of the 7th PDZ domain of MPDZ (MUPP-1)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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