Related ArticlesThe conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism.
Biochim Biophys Acta. 2005 Feb 1;1668(1):1-9
Authors: Choi G, Guo J, Makriyannis A
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous GPCRs such as rhodopsin and the beta-adrenergic receptor exhibits unique structural and functional characteristics. Computational models also predict the existence of such a structural motif within the CB1 cannabinoid receptor, another member of the G-protein coupled receptor superfamily. To gain insights into the conformational properties of this GPCR component, a peptide corresponding to helix 8 of the CB1 receptor with a small contiguous segment from transmembrane helix 7 (TM7) was chemically synthesized and its secondary structure determined by circular dichroism (CD) and solution NMR spectroscopy. Our studies in DPC and SDS micelles revealed significant alpha-helical structure while in an aqueous medium, the peptide exhibited a random coil configuration. The relative orientation of helix 8 within the CB1 receptor was obtained from intermolecular 31P-1H and 1H-1H NOE measurements. Our results suggest that in the presence of an amphipathic membrane environment, helix 8 assumes an alpha helical structure with an orientation parallel to the phospholipid membrane surface and perpendicular to TM7. In this model, positively charged side chains interact with the lipid headgroups while the other polar side chains face the aqueous region. The above observations may be relevant to the activation/deactivation of the CB1 receptor.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
The interaction of cannabinoid receptor agonists, CP55940 and WIN55212-2 with membranes using solid state 2H NMR.
Biochim Biophys Acta. 2011 Sep;1808(9):2095-101
Authors: Tian X, Pavlopoulos S, Yang DP, Makriyannis A
Abstract
Two key commonly used cannabinergic agonists, CP55940 and WIN55212-2, are investigated for their effects on the lipid membrane bilayer using (2)H solid state NMR, and the results are compared with our...
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09-13-2011 08:27 PM
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Protein Pept Lett. 2011 Mar;18(3):318-26
Authors: Miura Y
Temperature dependence of the ?-helix conformation of bee venom melittin in methanol-water mixed solvents has been examined by NMR, in order to elucidate conformation stability and a phase diagram. At high methanol concentration of 100 - ca. 80 wt.%, melittin forms a full ?-helix conformation in the...
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06-04-2011 11:26 AM
[NMR paper] Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor:
Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study.
Related Articles Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study.
Biochim Biophys Acta. 2004 May 27;1663(1-2):74-81
Authors: Katragadda M, Maciejewski MW, Yeagle PL
The recently reported crystal structure of bovine rhodopsin revealed a cytoplasmic helix (helix 8) in addition to the seven transmembrane helices. This domain is roughly perpendicular to the transmembrane bundle in the presence of an...
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11-24-2010 09:51 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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11-24-2010 09:16 PM
[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%...
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11-24-2010 09:01 PM
[NMR paper] The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular
The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
Related Articles The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
J Pept Res. 2002 Sep;60(3):169-77
Authors: Choi G, Landin J, Xie XQ
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous G protein-coupled receptors (GPCRs) such as rhodopsin and...
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11-24-2010 08:58 PM
[NMR paper] Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Related Articles Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Mol Membr Biol. 1994 Oct-Dec;11(4):263-9
Authors: Hubbard JA, MacLachlan LK, Meenan E, Salter CJ, Reid DG, Lahouratate P, Humphries J, Stevens N, Bell D, Neville WA
Nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy have been used to characterize the conformation of the putative cytoplasmic domain of phospholamban (PLB), an oligomeric membrane-bound protein which...
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08-22-2010 03:29 AM
[KPWU blog] [IDP] Cytoplasmic Domain of the T Cell Receptor zeta
Cytoplasmic Domain of the T Cell Receptor zeta
Title:* The Intrinsically Disordered Cytoplasmic Domain of the T Cell Receptor ? Chain Binds to the Nef Protein of Simian Immunodeficiency Virus without a Disorder-to-Order Transition Authors: Alexander B. Sigalov, Walter M. Kim, Maria Saline and Lawrence J. Stern Journal: Biochemistry, 2008, 47 (49), pp 12942–12944 Not fully labeled in HSQChttp://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=197&subd=kpwu&ref=&feed=1
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