2qbw

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[[Image:2qbw.jpg|left|200px]]
 
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==The crystal structure of PDZ-Fibronectin fusion protein==
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The line below this paragraph, containing "STRUCTURE_2qbw", creates the "Structure Box" on the page.
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<StructureSection load='2qbw' size='340' side='right'caption='[[2qbw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qbw]] 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=2QBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QBW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#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=2qbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qbw OCA], [https://pdbe.org/2qbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qbw RCSB], [https://www.ebi.ac.uk/pdbsum/2qbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qbw ProSAT]</span></td></tr>
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{{STRUCTURE_2qbw| PDB=2qbw | SCENE= }}
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</table>
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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/qb/2qbw_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=2qbw ConSurf].
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<div style="clear:both"></div>
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'''The crystal structure of PDZ-Fibronectin fusion protein'''
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==See Also==
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*[[Fibronectin 3D structures|Fibronectin 3D structures]]
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== References ==
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==Overview==
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<references/>
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Most natural proteins performing sophisticated tasks contain multiple domains where an active site is located at the domain interface. Comparative structural analyses suggest that major leaps in protein function occur through gene recombination events that connect two or more protein domains to generate a new active site, frequently occurring at the newly created domain interface. However, such functional leaps by combination of unrelated domains have not been directly demonstrated. Here we show that highly specific and complex protein functions can be generated by joining a low-affinity peptide-binding domain with a functionally inert second domain and subsequently optimizing the domain interface. These directed evolution processes dramatically enhanced both affinity and specificity to a level unattainable with a single domain, corresponding to &gt;500-fold and &gt;2,000-fold increases of affinity and specificity, respectively. An x-ray crystal structure revealed that the resulting "affinity clamp" had clamshell architecture as designed, with large additional binding surface contributed by the second domain. The affinity clamps having a single-nanomolar dissociation constant outperformed a monoclonal antibody in immunochemical applications. This work establishes evolutionary paths from isolated domains with primitive function to multidomain proteins with sophisticated function and introduces a new protein-engineering concept that allows for the generation of highly functional affinity reagents to a predefined target. The prevalence and variety of natural interaction domains suggest that numerous new functions can be designed by using directed domain interface evolution.
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__TOC__
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</StructureSection>
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==About this Structure==
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2QBW is a [[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=2QBW OCA].
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==Reference==
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Design of protein function leaps by directed domain interface evolution., Huang J, Koide A, Makabe K, Koide S, Proc Natl Acad Sci U S A. 2008 May 6;105(18):6578-83. Epub 2008 Apr 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18445649 18445649]
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[[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: Huang, J.]]
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[[Category: Huang J]]
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[[Category: Koide, A.]]
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[[Category: Koide A]]
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[[Category: Koide, S.]]
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[[Category: Koide S]]
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[[Category: Makabe, K.]]
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[[Category: Makabe K]]
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[[Category: Fibronectin pdz]]
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[[Category: Unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:39:04 2008''
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Current revision

The crystal structure of PDZ-Fibronectin fusion protein

PDB ID 2qbw

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