2l9u
From Proteopedia
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==Spatial structure of dimeric ErbB3 transmembrane domain== | ==Spatial structure of dimeric ErbB3 transmembrane domain== | ||
<StructureSection load='2l9u' size='340' side='right' caption='[[2l9u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2l9u' size='340' side='right' caption='[[2l9u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2l9u]] is a 2 chain structure | + | <table><tr><td colspan='2'>[[2l9u]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9U FirstGlance]. <br> |
| - | </td></tr> | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></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=2l9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9u OCA], [http://pdbe.org/2l9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9u RCSB], [http://www.ebi.ac.uk/pdbsum/2l9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9u ProSAT]</span></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=2l9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9u OCA], [http://pdbe.org/2l9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9u RCSB], [http://www.ebi.ac.uk/pdbsum/2l9u PDBsum]</span></td></tr> | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ERBB3_HUMAN ERBB3_HUMAN]] Binds and is activated by neuregulins and NTAK.<ref>PMID:15358134</ref> | [[http://www.uniprot.org/uniprot/ERBB3_HUMAN ERBB3_HUMAN]] Binds and is activated by neuregulins and NTAK.<ref>PMID:15358134</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In present work the interaction of two TM alpha-helices of the ErbB3 receptor tyrosine kinase from the ErbB or HER family (residues 639-670) was studied by means of NMR spectroscopy in a membrane-mimicking environment provided by the DPC micelles. The ErbB3 TM segment appeared to form a parallel symmetric dimer in a left-handed orientation. The interaction between TM spans is accomplished via the non-standard motif and is supported by apolar contacts of bulky side chains and by stacking of aromatic rings together with pi-cation interactions of Phe and Arg side chains. The investigation of the dimer--monomer equilibrium revealed thermodynamic properties of the assembly and the presence of two distinct regimes of the dimerization at low and at high peptide/detergent ratio. It was found that the detergent in case of ErbB3 behaves not as an ideal solvent, thus affecting the dimer--monomer equilibrium. Such behavior may account for the problems occurring with the refolding and stability of multispan helical membrane proteins in detergent solutions. The example of ErbB3 allows us to conclude that the thermodynamic parameters of dimerization, measured in micelles for two different helical pairs, cannot be compared without the investigation of their dependence on detergent concentration. | ||
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| + | Spatial structure and dimer--monomer equilibrium of the ErbB3 transmembrane domain in DPC micelles.,Mineev KS, Khabibullina NF, Lyukmanova EN, Dolgikh DA, Kirpichnikov MP, Arseniev AS Biochim Biophys Acta. 2011 Aug;1808(8):2081-8. doi: 10.1016/j.bbamem.2011.04.017., Epub 2011 May 6. PMID:21575594<ref>PMID:21575594</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2l9u" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Human]] | ||
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
[[Category: Arseniev, A S]] | [[Category: Arseniev, A S]] | ||
Revision as of 03:43, 6 September 2017
Spatial structure of dimeric ErbB3 transmembrane domain
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