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4xh7

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Revision as of 00:20, 26 January 2017

Crystal structure of MUPP1 PDZ4

Structural highlights

4xh7 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Publication Abstract from PubMed

Specific protein-protein interactions are important for biological signal transduction. The postsynaptic density-95, disc-large, and zonulin-1 (PDZ) domain is one of the most abundant protein interaction modules. Multi-PDZ-domain protein 1 (MUPP1), as a scaffold protein, contains 13 PDZ domains and plays an important role in cytoskeletal organization, cell polarity, and cell proliferation. The study on PDZ domain of MUPP1 helps to understand the mechanisms and functions of MUPP1. In the present study, the fourth PDZ domain of MUPP1 (MUPP1-PDZ4) from Mus musculus was cloned, expressed, purified, and characterized. The MUPP1-PDZ4 domain was subcloned into a pET-vector and expressed in Escherichia coli. Affinity chromatography and size-exclusion chromatography were used to purify the protein. MUPP1-PDZ4 protein was a monomer with a molar mass of 16.4 kDa in solution and had a melting point of 60.3 degrees C. Using the sitting-drop vapor-diffusion method, MUPP1-PDZ4 protein crystals were obtained in a solution (pH 7.0) containing 2% (v/v) polyethylene glycol 400, 0.1 M imidazole, and 24% (w/v) polyethylene glycol monoethyl ether 5000. Finally, the crystal was diffracted with 1.6 A resolution. The crystal structure showed that MUPP1-PDZ4 domain contained three alpha-helices and six beta-strands in the core. The GLGI motif, L562/A564 on the beta-strand B, and H605/V608/L612 on the alpha-helix B formed a PDZ binding pocket which could bind to the C-terminal of the binding partners. This biochemical and structural information will provide insights into how PDZ binds to its target peptide and the theoretical foundation for the function of MUPP1.

Biochemical and structural characterization of MUPP1-PDZ4 domain from Mus musculus.,Zhu H, Liu Z, Huang Y, Zhang C, Li G, Liu W Acta Biochim Biophys Sin (Shanghai). 2015 Mar;47(3):199-206. doi:, 10.1093/abbs/gmv002. Epub 2015 Feb 7. PMID:25662616^[1]

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

References

↑ Zhu H, Liu Z, Huang Y, Zhang C, Li G, Liu W. Biochemical and structural characterization of MUPP1-PDZ4 domain from Mus musculus. Acta Biochim Biophys Sin (Shanghai). 2015 Mar;47(3):199-206. doi:, 10.1093/abbs/gmv002. Epub 2015 Feb 7. PMID:25662616 doi:http://dx.doi.org/10.1093/abbs/gmv002

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xh7"

@@ Line 1: / Line 1: @@
 ==Crystal structure of MUPP1 PDZ4==
 <StructureSection load='4xh7' size='340' side='right' caption='[[4xh7]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4xh7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XH7 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></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=4xh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xh7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh7 PDBsum]</span></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=4xh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh7 OCA], [http://pdbe.org/4xh7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xh7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xh7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4xh7

From Proteopedia

Revision as of 00:20, 26 January 2017

Crystal structure of MUPP1 PDZ4

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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