Related ArticlesThe 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 the beta-adrenergic receptor exhibit unique structural and functional characteristics. Computer models also predict this structure for the cannabinoid CB2 receptor, another member of the GPCR superfamily. In our study, a peptide corresponding to helix 8 of the CB2 receptor was synthesized chemically and its secondary structure determined by circular dichroism (CD) and (1)H NMR spectroscopy. NMR and CD revealed an alpha-helical structure in this region in both dodecylphosphocholine micelles and dimethylsulfoxide, in contrast to a random coil configuration found in aqueous solvent. This finding is in good agreement with other previous GPCR structural studies including X-ray crystallography. By combining our finding with other studies, we further hypothesize that the amphipathic nature of helix 8 can play a significant role in the function and regulation of CB receptors as well as other GPCRs in general.
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
[NMR paper] The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR
The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism.
Related Articles The 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...
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11-24-2010 11:14 PM
[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] An NMR and circular dichroism study of the interaction of thiocyanate with human and
An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Related Articles An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Biophys Chem. 2003 Dec 1;106(3):233-40
Authors: Sau AK, Currell D, Mazumdar S, Mitra S
The interaction of thiocyanate with human native and cross-linked...
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11-24-2010 09:16 PM
[NMR paper] Investigating the conformational coupling between the transmembrane and cytoplasmic d
Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
Related Articles Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
FEBS Lett. 2001 Sep 21;505(3):431-5
Authors: Mousson F, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively...
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11-19-2010 08:44 PM
[NMR paper] Conformational changes in the human estrogen receptor observed by (19)F NMR.
Conformational changes in the human estrogen receptor observed by (19)F NMR.
Related Articles Conformational changes in the human estrogen receptor observed by (19)F NMR.
Biochem Biophys Res Commun. 2000 Apr 21;270(3):988-91
Authors: Luck LA, Barse JL, Luck AM, Peck CH
The (19)F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282-595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the...
[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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The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular
Linear Mode
