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1pjd
From Proteopedia
(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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| - | [[Image:1pjd.jpg|left|200px]]<br /><applet load="1pjd" size=" | + | [[Image:1pjd.jpg|left|200px]]<br /><applet load="1pjd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pjd" /> | caption="1pjd" /> | ||
'''Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers'''<br /> | '''Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A detailed analysis of the structure of an 18-residue peptide | + | 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== | ==About this Structure== | ||
| - | 1PJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1PJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJD OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arshava, B.]] | [[Category: Arshava, B.]] | ||
| - | [[Category: Becker, J | + | [[Category: Becker, J M.]] |
| - | [[Category: Ding, F | + | [[Category: Ding, F X.]] |
| - | [[Category: Liu, S | + | [[Category: Liu, S F.]] |
| - | [[Category: Marassi, F | + | [[Category: Marassi, F M.]] |
[[Category: Naider, F.]] | [[Category: Naider, F.]] | ||
| - | [[Category: Nevzorov, A | + | [[Category: Nevzorov, A A.]] |
| - | [[Category: Opella, S | + | [[Category: Opella, S J.]] |
| - | [[Category: Valentine, K | + | [[Category: Valentine, K G.]] |
[[Category: Veglia, G.]] | [[Category: Veglia, G.]] | ||
| - | [[Category: Wang, S | + | [[Category: Wang, S H.]] |
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:28 2008'' |
Revision as of 12:29, 21 February 2008
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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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