1iox: Difference between revisions

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New page: left|200px<br /> <applet load="1iox" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iox" /> '''NMR Structure of human Betacellulin-2'''<br...
 
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[[Image:1iox.gif|left|200px]]<br />
<applet load="1iox" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iox" />
'''NMR Structure of human Betacellulin-2'''<br />


==Overview==
==NMR Structure of human Betacellulin-2==
The solution structure of the EGF-like domain of betacellulin (BTCe), a, newly discovered member of the epidermal growth factor (EGF) family, has, been determined using two-dimensional nuclear magnetic resonance, spectroscopy. This is the first report to identify the solution structure, of the EGF-family ligand monomers that interact with both ErbB-1 and, ErbB-4. The solution structure of BTCe was calculated using 538, NMR-derived restraints. The overall structure of BTCe was stabilized by, three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It, appears that BTCe is comprised of five beta-strands and one short 3(10), helical turn. The secondary structural elements of BTCe are basically, similar to those of the other EGF-family proteins, except that several, significant variations of the structural properties were found. It is, suggested that the structural variations between BTCe and the other, EGF-family ligands may affect the specific receptor-recognition properties, of EGF-family ligands.
<StructureSection load='1iox' size='340' side='right'caption='[[1iox]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iox]] 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=1IOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOX FirstGlance]. <br>
</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=1iox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iox OCA], [https://pdbe.org/1iox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iox RCSB], [https://www.ebi.ac.uk/pdbsum/1iox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iox ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BTC_HUMAN BTC_HUMAN] Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.<ref>PMID:8570211</ref>
== 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/io/1iox_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=1iox ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the EGF-like domain of betacellulin (BTCe), a newly discovered member of the epidermal growth factor (EGF) family, has been determined using two-dimensional nuclear magnetic resonance spectroscopy. This is the first report to identify the solution structure of the EGF-family ligand monomers that interact with both ErbB-1 and ErbB-4. The solution structure of BTCe was calculated using 538 NMR-derived restraints. The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It appears that BTCe is comprised of five beta-strands and one short 3(10) helical turn. The secondary structural elements of BTCe are basically similar to those of the other EGF-family proteins, except that several significant variations of the structural properties were found. It is suggested that the structural variations between BTCe and the other EGF-family ligands may affect the specific receptor-recognition properties of EGF-family ligands.


==About this Structure==
Solution structure of betacellulin, a new member of EGF-family ligands.,Miura K, Doura H, Aizawa T, Tada H, Seno M, Yamada H, Kawano K Biochem Biophys Res Commun. 2002 Jun 28;294(5):1040-6. PMID:12074582<ref>PMID:12074582</ref>
1IOX 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=1IOX OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of betacellulin, a new member of EGF-family ligands., Miura K, Doura H, Aizawa T, Tada H, Seno M, Yamada H, Kawano K, Biochem Biophys Res Commun. 2002 Jun 28;294(5):1040-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12074582 12074582]
</div>
<div class="pdbe-citations 1iox" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aizawa, T.]]
[[Category: Aizawa T]]
[[Category: Doura, H.]]
[[Category: Doura H]]
[[Category: Kawano, K.]]
[[Category: Kawano K]]
[[Category: Miura, K.]]
[[Category: Miura K]]
[[Category: Seno, M.]]
[[Category: Seno M]]
[[Category: Tada, H.]]
[[Category: Tada H]]
[[Category: Yamada, H.]]
[[Category: Yamada H]]
[[Category: egf-like fold]]
 
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