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1mfg

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[[Image:1mfg.gif|left|200px]]<br /><applet load="1mfg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mfg, resolution 1.25&Aring;" />
 
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'''The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor'''<br />
 
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==Overview==
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==The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor==
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Erbin contains a class I PDZ domain that binds to the C-terminal region of the receptor tyrosine kinase ErbB2, a class II ligand. The crystal structure of the human Erbin PDZ bound to the peptide EYLGLDVPV corresponding to the C-terminal residues 1247-1255 of human ErbB2 has been determined at 1.25-A resolution. The Erbin PDZ deviates from the canonical PDZ fold in that it contains a single alpha-helix. The isopropyl group of valine at position -2 of the ErbB2 peptide interacts with the Erbin Val(1351) and displaces the peptide backbone away from the alpha-helix, elucidating the molecular basis of class II ligand recognition by a class I PDZ domain. Strikingly, the phenolic ring of tyrosine -7 enters into a pocket formed by the extended beta 2-beta 3 loop of the Erbin PDZ. Phosphorylation of tyrosine -7 abolishes this interaction but does not affect the binding of the four C-terminal peptidic residues to PDZ, as revealed by the crystal structure of the Erbin PDZ complexed with a phosphotyrosine-containing ErbB2 peptide. Since phosphorylation of tyrosine -7 plays a critical role in ErbB2 function, the selective binding and sequestration of this residue in its unphosphorylated state by the Erbin PDZ provides a novel mechanism for regulation of the ErbB2-mediated signaling and oncogenicity.
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<StructureSection load='1mfg' size='340' side='right'caption='[[1mfg]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1mfg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MFG FirstGlance]. <br>
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1MFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFG OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfg OCA], [https://pdbe.org/1mfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mfg RCSB], [https://www.ebi.ac.uk/pdbsum/1mfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mfg ProSAT]</span></td></tr>
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==Reference==
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</table>
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Novel mode of ligand recognition by the Erbin PDZ domain., Birrane G, Chung J, Ladias JA, J Biol Chem. 2003 Jan 17;278(3):1399-402. Epub 2002 Nov 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12444095 12444095]
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== Function ==
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[https://www.uniprot.org/uniprot/ERBIN_HUMAN ERBIN_HUMAN] Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728).<ref>PMID:10878805</ref> <ref>PMID:16203728</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mf/1mfg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mfg ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Birrane, G.]]
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[[Category: Birrane G]]
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[[Category: Chung, J.]]
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[[Category: Chung J]]
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[[Category: Ladias, J A.]]
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[[Category: Ladias JA]]
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[[Category: erb-b2]]
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[[Category: erbin.]]
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[[Category: pdz domain]]
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[[Category: protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:45 2008''
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Current revision

The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor

PDB ID 1mfg

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