1iij

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[[Image:1iij.png|left|200px]]
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==SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT==
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<StructureSection load='1iij' size='340' side='right' caption='[[1iij]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iij]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IIJ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iij OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iij RCSB], [http://www.ebi.ac.uk/pdbsum/1iij PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1iij| PDB=1iij | SCENE= }}
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Evidence for an alpha-helix --&gt; 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<ref>PMID:11371217</ref>
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===SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_11371217}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1iij]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIJ OCA].
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</StructureSection>
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Bontems, F.]]
[[Category: Bontems, F.]]

Revision as of 10:39, 28 September 2014

SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT

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