Related ArticlesStructure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Biopolymers. 1998 Nov;46(6):343-57
Authors: Arshava B, Liu SF, Jiang H, Breslav M, Becker JM, Naider F
Peptides representing both loop and the sixth transmembrane regions of the alpha-factor receptor of Saccharomyces cerevisiae were synthesized by solid-phase procedures and purified to near homogeneity. CD, nmr, and modeling analysis indicated that in aqueous media the first extracellular loop peptide E1(107-125), the third intracellular loop peptide I3(231-243), and the carboxyl terminus peptide I4(350-372) were mostly disordered. In contrast, the second extracellular loop peptide E2(191-206) assumed a well-defined structure in aqueous medium and the sixth transmembrane domain peptide receptor M6(252-269, C252A) was highly helical in trifluoroethanol/water (4:1), exhibiting a kink at Pro258. A synthetic peptide containing a sequence similar to that of the sixth transmembrane domain of a constitutively active alpha-factor receptor M6(252-269, C252A, P258L) in which Leu replaces Pro258 exhibited significantly different biophysical properties than the wild-type sequence. In particular, this peptide had very low solubility and gave CD resembling that of a beta-sheet structure in hexafluoroacetone/water (1:1) whereas the wild-type peptide was partially helical under identical conditions. These results would be consistent with the hypothesis that the constitutive activity of the mutant receptor is linked to a conformational change in the sixth transmembrane domain. The study of the receptor segments also indicate that peptides corresponding to loops of the alpha-factor receptor do not appear to assume turn structures.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Biochim Biophys Acta. 2011 Jul 23;
Authors: Cohen LS, Arshava B, Neumoin A, Becker JM, Güntert P, Zerbe O, Naider F
Fragments of integral membrane proteins have been used to study the physical chemical properties of regions of transporters and receptors. Ste2p(G31-T110) is an 80-residue polypeptide which contains a...
[NMR paper] Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Related Articles Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Biochemistry. 2005 Sep 6;44(35):11795-810
Authors: Estephan R, Englander J, Arshava B, Samples KL, Becker JM, Naider F
The yeast Saccharomyces cerevisiae alpha-factor pheromone receptor (Ste2p) was used as a model G protein-coupled receptor (GPCR). A 73-mer multidomain fragment of Ste2p (residues 267-339)...
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[NMR paper] Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled r
Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
Related Articles Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
J Am Chem Soc. 2005 Jun 8;127(22):8010-1
Authors: Tian C, Breyer RM, Kim HJ, Karra MD, Friedman DB, Karpay A, Sanders CR
The seven-transmembrane-spanning G protein-coupled receptor (GPCR) superfamily plays many important roles in basic biology, human health, and human disease. Here, well-resolved solution NMR spectra are presented for a human...
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11-25-2010 08:21 PM
[NMR paper] Conformational analysis of peptide analogues of silkmoth chorion protein segments usi
Conformational analysis of peptide analogues of silkmoth chorion protein segments using CD, NMR and molecular modelling.
Related Articles Conformational analysis of peptide analogues of silkmoth chorion protein segments using CD, NMR and molecular modelling.
J Pept Sci. 2004 Jun;10(6):381-92
Authors: Benaki DC, Mikros E, Hamodrakas SJ
Silkmoth proteins secreted from the follicular cells that surround the oocyte form a large extracellular assembly which is important for protecting and sustaining the structure of the oocyte and the developing...
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11-24-2010 09:51 PM
[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Related Articles Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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11-24-2010 09:25 PM
[NMR paper] The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonis
The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonist involved in appetite regulation and sleep.
Related Articles The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonist involved in appetite regulation and sleep.
J Biomol Struct Dyn. 2003 Oct;21(2):201-10
Authors: Miskolzie M, Kotovych G
The conformation of orexin-A, an orphan G-protein coupled receptor agonist has been determined when bound to sodium dodecylsulphate-d(25) (SDS) micelles by (1)H and (13)C NMR and molecular...
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[NMR paper] The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor
The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Related Articles The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Biopolymers. 2003 Jun;69(2):201-15
Authors: Miskolzie M, Kotovych G
The tertiary structure of the pain modulating and anti-opiate neuropeptide, human neuropeptide AF (NPAF) (the sequence is AGEGLNSQFWSLAAPQRF-NH(2)), was determined by (1)H-NMR. The structure of NPAF was determined in two solvent systems, namely 50%/50%...
Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Sac
Linear Mode
