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1hj0

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[[Image:1hj0.jpg|left|200px]]<br /><applet load="1hj0" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hj0" />
 
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'''THYMOSIN BETA9'''<br />
 
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==Overview==
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==Thymosin beta9==
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The conformation of thymosin beta 9 in solution of 40% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol-d2 in water has been investigated by two-dimensional 1H-nmr spectroscopy. Under this condition thymosin beta 9 adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton distance constraints derived from nuclear Overhauser enhancement measurements. The conformation of thymosin beta 9 includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-terminus of thymosin beta 9 shows random-coil structure only.
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<StructureSection load='1hj0' size='340' side='right'caption='[[1hj0]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hj0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJ0 FirstGlance]. <br>
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1HJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJ0 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj0 OCA], [https://pdbe.org/1hj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hj0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hj0 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Conformation of thymosin beta 9 in water/fluoroalcohol solution determined by NMR spectroscopy., Stoll R, Voelter W, Holak TA, Biopolymers. 1997 May;41(6):623-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9108730 9108730]
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== Function ==
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[https://www.uniprot.org/uniprot/TYB10_BOVIN TYB10_BOVIN] Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
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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/hj/1hj0_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=1hj0 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Holak, T A.]]
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[[Category: Holak TA]]
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[[Category: Stoll, R.]]
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[[Category: Stoll R]]
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[[Category: Voelter, W.]]
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[[Category: Voelter W]]
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[[Category: actin]]
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[[Category: immunopotentiation]]
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[[Category: t-cell differentiation]]
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[[Category: thymus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:42 2008''
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Current revision

Thymosin beta9

PDB ID 1hj0

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