1iij
From Proteopedia
|
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
Page seeded by OCA on Tue Nov 20 17:25:32 2007
