4tgf: Difference between revisions

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New page: left|200px<br /> <applet load="4tgf" size="450" color="white" frame="true" align="right" spinBox="true" caption="4tgf" /> '''SOLUTION STRUCTURES OF HUMAN TRANSFORMING G...
 
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[[Image:4tgf.gif|left|200px]]<br />
<applet load="4tgf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="4tgf" />
'''SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA'''<br />


==Overview==
==SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA==
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human, transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3., The conformation space of des-Val-Val TGF-alpha was explored by distance, geometry embedding followed by restrained molecular dynamics refinement, using NOE distance constraints and some torsion angle constraints derived, from J-couplings. Over 80 long-range NOE constraints were found by, completely assigning all resolved cross-peaks in the NOESY spectra. Low, NOE constraint violations were observed in structures obtained with the, following three different refinement procedures: interactive annealing in, DSPACE, AMBER 3.0 restrained molecular dynamics, and dynamic simulated, annealing in XPLOR. The segment from Phe15 to Asp47 was found to be, conformationally well-defined. Back-calculations of NOESY spectra were, used to evaluate the quality of the structures. Our calculated structures, resemble the ribbon diagram presentations that were recently reported by, other groups. Several side-chain conformations appear to be well-defined, as does the relative orientation of the C loop to the N-terminal half of, the protein.
<StructureSection load='4tgf' size='340' side='right'caption='[[4tgf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tgf]] 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=4TGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TGF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 4 models</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=4tgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tgf OCA], [https://pdbe.org/4tgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tgf RCSB], [https://www.ebi.ac.uk/pdbsum/4tgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tgf 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/4tgf_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=4tgf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by restrained molecular dynamics refinement using NOE distance constraints and some torsion angle constraints derived from J-couplings. Over 80 long-range NOE constraints were found by completely assigning all resolved cross-peaks in the NOESY spectra. Low NOE constraint violations were observed in structures obtained with the following three different refinement procedures: interactive annealing in DSPACE, AMBER 3.0 restrained molecular dynamics, and dynamic simulated annealing in XPLOR. The segment from Phe15 to Asp47 was found to be conformationally well-defined. Back-calculations of NOESY spectra were used to evaluate the quality of the structures. Our calculated structures resemble the ribbon diagram presentations that were recently reported by other groups. Several side-chain conformations appear to be well-defined as does the relative orientation of the C loop to the N-terminal half of the protein.


==About this Structure==
Solution structures of human transforming growth factor alpha derived from 1H NMR data.,Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L Biochemistry. 1990 Aug 28;29(34):7805-13. PMID:2261437<ref>PMID:2261437</ref>
4TGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4TGF OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structures of human transforming growth factor alpha derived from 1H NMR data., Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L, Biochemistry. 1990 Aug 28;29(34):7805-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2261437 2261437]
</div>
<div class="pdbe-citations 4tgf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brown, F.K.]]
[[Category: Brown FK]]
[[Category: Brown, S.C.]]
[[Category: Brown SC]]
[[Category: Jeffs, P.W.]]
[[Category: Jeffs PW]]
[[Category: Kline, T.P.]]
[[Category: Kline TP]]
[[Category: Kopple, K.D.]]
[[Category: Kopple KD]]
[[Category: Mueller, L.]]
[[Category: Mueller L]]
[[Category: growth factor]]
 
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Latest revision as of 03:33, 21 November 2024

SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA

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