View source for 2tgf


==THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA==
<StructureSection load='2tgf' size='340' side='right'caption='[[2tgf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2tgf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TGF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2tgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tgf OCA], [https://pdbe.org/2tgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tgf RCSB], [https://www.ebi.ac.uk/pdbsum/2tgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tgf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TGFA_HUMAN TGFA_HUMAN] TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
== 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/tg/2tgf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2tgf ConSurf].
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== Publication Abstract from PubMed ==
The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made.

The solution structure of human transforming growth factor alpha.,Harvey TS, Wilkinson AJ, Tappin MJ, Cooke RM, Campbell ID Eur J Biochem. 1991 Jun 15;198(3):555-62. PMID:2050136<ref>PMID:2050136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Campbell ID]]
[[Category: Cooke RM]]
[[Category: Harvey TS]]
[[Category: Tappin MJ]]
[[Category: Wilkinson AJ]]