View source for 3tgf


==THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA==
<StructureSection load='3tgf' size='340' side='right'caption='[[3tgf]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tgf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TGF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2tgf|2tgf]]</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=3tgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tgf OCA], [http://pdbe.org/3tgf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tgf RCSB], [http://www.ebi.ac.uk/pdbsum/3tgf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tgf ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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/3tgf_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=3tgf 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: Human]]
[[Category: Large Structures]]
[[Category: Campbell, I D]]
[[Category: Cooke, R M]]
[[Category: Harvey, T S]]
[[Category: Tappin, M J]]
[[Category: Wilkinson, A J]]
[[Category: Growth factor]]