| Title: | Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers |
| Author(s): | Valentine KG; Liu SF; Marassi FM; Veglia G; Opella SJ; Ding FX; Wang SH; Arshava B; Becker JM; Naider F; |
| Address: | "Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA" |
| DOI: | 10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H |
| ISSN/ISBN: | 0006-3525 (Print) 1097-0282 (Electronic) 0006-3525 (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Biopolymers/chemistry/genetics Lipid Bilayers Magnetic Resonance Spectroscopy Mating Factor Models, Molecular Molecular Sequence Data Nitrogen Isotopes Peptides/chemistry Phospholipids Protein Structure, Tertiary Receptors, Mating Fact;" |
| Notes: | "MedlineValentine, K G Liu, S F Marassi, F M Veglia, G Opella, S J Ding, F X Wang, S H Arshava, B Becker, J M Naider, F eng R01 GM022087/GM/NIGMS NIH HHS/ P41 RR009793-06/RR/NCRR NIH HHS/ R01 GM022086/GM/NIGMS NIH HHS/ GM 22086/GM/NIGMS NIH HHS/ P41RR09731/RR/NCRR NIH HHS/ R56 GM022086/GM/NIGMS NIH HHS/ GM 22087/GM/NIGMS NIH HHS/ R56 GM022087/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 2001/07/27 Biopolymers. 2001 Oct 5; 59(4):243-56. doi: 10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO; 2-H" |
