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==Thymosin beta9==
==Thymosin beta9==
<StructureSection load='1hj0' size='340' side='right'caption='[[1hj0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1hj0' size='340' side='right'caption='[[1hj0]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1hj0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Holak, T A]]
[[Category: Holak TA]]
[[Category: Stoll, R]]
[[Category: Stoll R]]
[[Category: Voelter, W]]
[[Category: Voelter W]]
[[Category: Actin]]
[[Category: Actin binding peptide]]
[[Category: Immunopotentiation]]
[[Category: T-cell differentiation]]
[[Category: Thymus]]

Latest revision as of 14:32, 27 March 2024

Thymosin beta9Thymosin beta9

Structural highlights

1hj0 is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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OCA
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