G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the best-studied member of this superfamily. Here, we provide the first evidence that activation in rhodopsin may involve differential dynamic properties of side-chain versus backbone atoms. High-resolution NMR studies of alpha-(15)N-labeled receptor revealed large backbone motions in the inactive dark state. In contrast, indole side-chain (15)N groups of tryptophans showed well resolved, equally intense NMR signals, suggesting restriction to a single specific conformation.
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Abstract Siderocalin Q83 is a small soluble protein that has the ability to bind two different ligands (enterobactin and arachidonic acid) simultaneously in two distinct binding sites. Here we report that Q83 exhibits an intriguing dynamic behavior. In its free form, the protein undergoes significant micro-to-millisecond dynamics. When binding arachidonic acid, the motions of the arachidonic acid binding site are quenched while the dynamics at the enterobactin binding site increases. Reciprocally, enterobactin...
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09-30-2011 08:01 PM
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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12-01-2010 06:56 PM
[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] 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] Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Sac
Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Related Articles Structure 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...