1pjd: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pjd]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PJD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pjd]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PJD FirstGlance]. <br> | ||
</td></tr><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=1pjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pjd RCSB], [http://www.ebi.ac.uk/pdbsum/1pjd PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pjd RCSB], [http://www.ebi.ac.uk/pdbsum/1pjd PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/STE2_YEAST STE2_YEAST]] Receptor for the peptide pheromone alpha factor, the mating factor of yeast. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arshava, B | [[Category: Arshava, B]] | ||
[[Category: Becker, J M | [[Category: Becker, J M]] | ||
[[Category: Ding, F X | [[Category: Ding, F X]] | ||
[[Category: Liu, S F | [[Category: Liu, S F]] | ||
[[Category: Marassi, F M | [[Category: Marassi, F M]] | ||
[[Category: Naider, F | [[Category: Naider, F]] | ||
[[Category: Nevzorov, A A | [[Category: Nevzorov, A A]] | ||
[[Category: Opella, S J | [[Category: Opella, S J]] | ||
[[Category: Valentine, K G | [[Category: Valentine, K G]] | ||
[[Category: Veglia, G | [[Category: Veglia, G]] | ||
[[Category: Wang, S H | [[Category: Wang, S H]] | ||
[[Category: Alpha helix]] | [[Category: Alpha helix]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 22:52, 25 December 2014
Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid BilayersStructure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers
Structural highlights
Function[STE2_YEAST] Receptor for the peptide pheromone alpha factor, the mating factor of yeast. Publication Abstract from PubMedA 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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