1iij
From Proteopedia
(New page: 200px<br /><applet load="1iij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iij" /> '''SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRAN...) |
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| - | [[Image:1iij.jpg|left|200px]]<br /><applet load="1iij" size=" | + | [[Image:1iij.jpg|left|200px]]<br /><applet load="1iij" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iij" /> | caption="1iij" /> | ||
'''SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT'''<br /> | '''SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 35-residue peptide corresponding to the very hydrophobic transmembrane | + | The 35-residue peptide corresponding to the very hydrophobic transmembrane region of the tyrosine kinase receptor neu, Neu(TM35), has been synthesized. The peptide can be solubilized in millimolar concentrations in TFE or incorporated into an SDS-water micellar solution or into well-hydrated DMPC/DCPC bicelles. In all these media, circular dichroism demonstrated that the peptide adopts a helical structure for about 80% of its amino acids. The peptide is monomeric below 2 mM in TFE, as also determined by variable concentration experiments. The three-dimensional solution structure in TFE has been obtained by homonuclear proton NMR and shows a well-defined alpha-helix from residues 4 to 21, then a pi-bulge from Ile(22) to Gly(28), and a final short alpha-helix from positions 29 to 32. This experimental finding is in agreement with structures predicted recently by molecular dynamics calculations in a vacuum [Sajot, N., and Genest, M. (2000) Eur. Biophys. J. 28, 648-662]. The biological implications of a possible retention of this structure in a membrane environment are finally discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1IIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http:// | + | 1IIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bontems, F.]] | [[Category: Bontems, F.]] | ||
[[Category: Carlotti, C.]] | [[Category: Carlotti, C.]] | ||
| - | [[Category: Dufourc, E | + | [[Category: Dufourc, E J.]] |
[[Category: Goetz, M.]] | [[Category: Goetz, M.]] | ||
[[Category: alpha-helix-pi-bulge-alpha-helix]] | [[Category: alpha-helix-pi-bulge-alpha-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:12 2008'' |
Revision as of 11:12, 21 February 2008
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SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT
Overview
The 35-residue peptide corresponding to the very hydrophobic transmembrane region of the tyrosine kinase receptor neu, Neu(TM35), has been synthesized. The peptide can be solubilized in millimolar concentrations in TFE or incorporated into an SDS-water micellar solution or into well-hydrated DMPC/DCPC bicelles. In all these media, circular dichroism demonstrated that the peptide adopts a helical structure for about 80% of its amino acids. The peptide is monomeric below 2 mM in TFE, as also determined by variable concentration experiments. The three-dimensional solution structure in TFE has been obtained by homonuclear proton NMR and shows a well-defined alpha-helix from residues 4 to 21, then a pi-bulge from Ile(22) to Gly(28), and a final short alpha-helix from positions 29 to 32. This experimental finding is in agreement with structures predicted recently by molecular dynamics calculations in a vacuum [Sajot, N., and Genest, M. (2000) Eur. Biophys. J. 28, 648-662]. The biological implications of a possible retention of this structure in a membrane environment are finally discussed.
About this Structure
1IIJ is a Single protein structure of sequence from [1]. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Evidence for an alpha-helix --> pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment. A 1H NMR and circular dichroism study., Goetz M, Carlotti C, Bontems F, Dufourc EJ, Biochemistry. 2001 May 29;40(21):6534-40. PMID:11371217
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