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1pjd

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Revision as of 09:30, 8 September 2021

Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers

Structural highlights

1pjd is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[STE2_YEAST] Receptor for the peptide pheromone alpha factor, the mating factor of yeast.

Publication Abstract from PubMed

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.

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

↑ Valentine KG, Liu SF, Marassi FM, Veglia G, Opella SJ, Ding FX, Wang SH, Arshava B, Becker JM, Naider F. Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers. Biopolymers. 2001 Oct 5;59(4):243-56. PMID:11473349 doi:<243::AID-BIP1021>3.0.CO;2-H http://dx.doi.org/10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pjd"

@@ Line 3: / Line 3: @@
 <StructureSection load='1pjd' size='340' side='right'caption='[[1pjd]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == 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 [https://proteopedia.org/fgij/fg.htm?mol=1PJD FirstGlance]. <br>
-</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://pdbe.org/1pjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pjd RCSB], [http://www.ebi.ac.uk/pdbsum/1pjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjd ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjd OCA], [https://pdbe.org/1pjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pjd RCSB], [https://www.ebi.ac.uk/pdbsum/1pjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/STE2_YEAST STE2_YEAST]] Receptor for the peptide pheromone alpha factor, the mating factor of yeast.
+[[https://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;">
 == Publication Abstract from PubMed ==

1pjd

From Proteopedia

Revision as of 09:30, 8 September 2021

Structure and Topology of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor in Phospholipid Bilayers

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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