1ktz

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[[Image:1ktz.gif|left|200px]]
 
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==Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3==
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The line below this paragraph, containing "STRUCTURE_1ktz", creates the "Structure Box" on the page.
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<StructureSection load='1ktz' size='340' side='right'caption='[[1ktz]], [[Resolution|resolution]] 2.15&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'>[[1ktz]] 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=1KTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTZ 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]] 2.15&#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=1ktz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktz OCA], [https://pdbe.org/1ktz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktz RCSB], [https://www.ebi.ac.uk/pdbsum/1ktz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktz ProSAT]</span></td></tr>
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{{STRUCTURE_1ktz| PDB=1ktz | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/TGFB3_HUMAN TGFB3_HUMAN] Defects in TGFB3 are a cause of familial arrhythmogenic right ventricular dysplasia type 1 (ARVD1) [MIM:[https://omim.org/entry/107970 107970]; also known as arrhythmogenic right ventricular cardiomyopathy 1 (ARVC1). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.<ref>PMID:15639475</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/TGFB3_HUMAN TGFB3_HUMAN] Involved in embryogenesis and cell differentiation.
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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/kt/1ktz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ktz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transforming growth factor-beta (TGF-beta) is the prototype of a large family of structurally related cytokines that play key roles in maintaining cellular homeostasis by signaling through two classes of functionally distinct Ser/Thr kinase receptors, designated as type I and type II. TGF-beta initiates receptor assembly by binding with high affinity to the type II receptor. Here, we present the 2.15 A crystal structure of the extracellular ligand-binding domain of the human TGF-beta type II receptor (ecTbetaR2) in complex with human TGF-beta3. ecTbetaR2 interacts with homodimeric TGF-beta3 by binding identical finger segments at opposite ends of the growth factor. Relative to the canonical 'closed' conformation previously observed in ligand structures across the superfamily, ecTbetaR2-bound TGF-beta3 shows an altered arrangement of its monomeric subunits, designated the 'open' conformation. The mode of TGF-beta3 binding shown by ecTbetaR2 is compatible with both ligand conformations. This, in addition to the predicted mode for TGF-beta binding to the type I receptor ectodomain (ecTbetaR1), suggests an assembly mechanism in which ecTbetaR1 and ecTbetaR2 bind at adjacent positions on the ligand surface and directly contact each other via protein--protein interactions.
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'''Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3'''
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Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex.,Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP Nat Struct Biol. 2002 Mar;9(3):203-8. PMID:11850637<ref>PMID:11850637</ref>
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==Overview==
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Transforming growth factor-beta (TGF-beta) is the prototype of a large family of structurally related cytokines that play key roles in maintaining cellular homeostasis by signaling through two classes of functionally distinct Ser/Thr kinase receptors, designated as type I and type II. TGF-beta initiates receptor assembly by binding with high affinity to the type II receptor. Here, we present the 2.15 A crystal structure of the extracellular ligand-binding domain of the human TGF-beta type II receptor (ecTbetaR2) in complex with human TGF-beta3. ecTbetaR2 interacts with homodimeric TGF-beta3 by binding identical finger segments at opposite ends of the growth factor. Relative to the canonical 'closed' conformation previously observed in ligand structures across the superfamily, ecTbetaR2-bound TGF-beta3 shows an altered arrangement of its monomeric subunits, designated the 'open' conformation. The mode of TGF-beta3 binding shown by ecTbetaR2 is compatible with both ligand conformations. This, in addition to the predicted mode for TGF-beta binding to the type I receptor ectodomain (ecTbetaR1), suggests an assembly mechanism in which ecTbetaR1 and ecTbetaR2 bind at adjacent positions on the ligand surface and directly contact each other via protein--protein interactions.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1KTZ is a [[Protein complex]] structure of sequences 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=1KTZ OCA].
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</div>
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<div class="pdbe-citations 1ktz" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex., Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP, Nat Struct Biol. 2002 Mar;9(3):203-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11850637 11850637]
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*[[TGF-beta receptor|TGF-beta receptor]]
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*[[TGF-beta receptor 3D structures|TGF-beta receptor 3D structures]]
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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: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Deep S]]
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[[Category: Deep, S.]]
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[[Category: Hart PJ]]
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[[Category: Hart, P J.]]
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[[Category: Hinck AP]]
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[[Category: Hinck, A P.]]
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[[Category: Hinck CS]]
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[[Category: Hinck, C S.]]
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[[Category: Shu Z]]
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[[Category: Shu, Z.]]
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[[Category: Taylor AB]]
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[[Category: Taylor, A B.]]
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[[Category: Cytokine-receptor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:10:10 2008''
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Current revision

Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3

PDB ID 1ktz

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