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1tgk

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[[Image:1tgk.gif|left|200px]]
 
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{{Structure
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==HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000==
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|PDB= 1tgk |SIZE=350|CAPTION= <scene name='initialview01'>1tgk</scene>, resolution 3.3&Aring;
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<StructureSection load='1tgk' size='340' side='right'caption='[[1tgk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1tgk]] is a 1 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=1TGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TGK FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.3&#8491;</td></tr>
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|GENE= HTGF-BETA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=1tgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgk OCA], [https://pdbe.org/1tgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tgk RCSB], [https://www.ebi.ac.uk/pdbsum/1tgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tgk ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgk OCA], [http://www.ebi.ac.uk/pdbsum/1tgk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tgk RCSB]</span>
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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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}}
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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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'''HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000'''
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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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==Overview==
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<jmolCheckbox>
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Transforming growth factors beta belong to a group of cytokines that control cellular proliferation and differentiation. Five isoforms are known that share approximately 75% sequence identity, but exert different biological activities. The structure of TGF-beta 3 was solved by X-ray crystallography and refined to a final R-factor of 17.5% at 2.0 A resolution. Comparison with the structure of TGF-beta 2 (Schlunegger MP, Grutter MG, 1992, Nature 358:430-434; Daopin S, Piez KA, Ogawa Y, Davies DR, 1992, Science 257:369-373) reveals a virtually identical central core. Differences exist in the conformations of the N-terminal alpha-helix and in the beta-sheet loops. In TGF-beta 3, the N-terminal alpha-helix has moved approximately 1 A away from the central core. This movement can be correlated with the mutation of Leu 17 to Val and Ala 47 to Pro in TGF-beta 3. The beta-sheet loops rotate as a rigid body 9 degrees around an axis that runs approximately parallel to the dimer axis. If these differences are recognized by the TGF-beta receptors, they might account for the individual cellular responses. A molecule of the precipitating agent dioxane is bound in a crystal contact, forming a hydrogen bond with Trp 32. This dioxane may occupy a carbohydrate-binding site, because dioxane possesses some structural similarity with a carbohydrate. The dioxane is in contact with two tryptophans, which are often involved in carbohydrate recognition.
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/1tgk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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==About this Structure==
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<text>to colour the structure by Evolutionary Conservation</text>
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1TGK 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=1TGK OCA].
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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=1tgk ConSurf].
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==Reference==
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<div style="clear:both"></div>
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The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding., Mittl PR, Priestle JP, Cox DA, McMaster G, Cerletti N, Grutter MG, Protein Sci. 1996 Jul;5(7):1261-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8819159 8819159]
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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: Gruetter, M G.]]
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[[Category: Gruetter MG]]
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[[Category: Mittl, P R.E.]]
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[[Category: Mittl PRE]]
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[[Category: Priestle, J P.]]
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[[Category: Priestle JP]]
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[[Category: glycoprotein]]
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[[Category: growth factor]]
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[[Category: mitogen]]
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[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:44 2008''
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HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000

PDB ID 1tgk

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