1pjd
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(New page: 200px<br /><applet load="1pjd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pjd" /> '''Structure and Topology of a Peptide Segment ...)
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Revision as of 00:28, 25 November 2007
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Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers
Overview
A detailed analysis of the structure of an 18-residue peptide, AQSLLVPSIIFILAYSLK [M6(252-269, C252A)] in, 1,2-dimyristoyl-sn-glycero-phosphocholine bilayers was carried out using, solid state NMR and attenuated total reflection Fourier transform infrared, spectroscopy. The peptide corresponds to a portion of the 6th, transmembrane domain of the alpha-factor receptor of Saccharomyces, cerevisiae. Ten homologs of M6(252-269, C252A) were synthesized in which, individual residues were labeled with (15)N. One- and two-dimensional, solid state NMR experiments were used to determine the chemical shifts and, (1)H-(15)N dipolar coupling constants for the (15)N-labeled peptides in, oriented dimyristoylphosphatidylcholine bilayers on stacked glass plates., These parameters were used to calculate the structure and orientation of, M6(252-269, C252A) in the bilayers. The results indicate that the carboxyl, terminal residues (9-14) are alpha-helical and oriented with an angle of, about 8 degrees with respect to the bilayer normal. Independently, an, attenuated total reflection Fourier transform infrared spectroscopy, analysis on M6(252-269, C252A) in a, 1,2-dimyristoyl-sn-glycero-phosphocholine bilayer concluded that the helix, tilt angle was about 12.5 degrees. The results on the structure of, M6(252-269, C252A) in bilayers are in good agreement with the structure, determined in trifluoroethanol/water solutions (B. Arshava et al., Biopolymers, 1998, Vol. 46, pp. 343-357). The present study shows that, solid state NMR spectroscopy can provide high resolution information on, the structure of transmembrane domains of a G protein-coupled receptor.
About this Structure
1PJD is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers., Valentine KG, Liu SF, Marassi FM, Veglia G, Opella SJ, Ding FX, Wang SH, Arshava B, Becker JM, Naider F, Biopolymers. 2001 Oct 5;59(4):243-56. PMID:11473349
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