View source for 1hj0


==Thymosin beta9==
<StructureSection load='1hj0' size='340' side='right' caption='[[1hj0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hj0]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HJ0 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj0 OCA], [http://pdbe.org/1hj0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hj0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hj0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hj0 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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). 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hj0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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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== Publication Abstract from PubMed ==
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.

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:9108730<ref>PMID:9108730</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1hj0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Holak, T A]]
[[Category: Stoll, R]]
[[Category: Voelter, W]]
[[Category: Actin]]
[[Category: Actin binding peptide]]
[[Category: Immunopotentiation]]
[[Category: T-cell differentiation]]
[[Category: Thymus]]