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. Author manuscript; available in PMC: 2010 Jan 5.
Published in final edited form as: Curr Pharm Des. 2009;15(35):4003–4016. doi: 10.2174/138161209789824803

Table 1.

A synoptic view of the available NMR structural data for GPCRs. A list of the abbreviations is provided in footnotea.

Receptor Source Domain Sequence Constraints Solvent Optimization Summary of Results Ref.
α2 adrenergic receptor human TM3-IL2-TM4 121–155 TMA DPC DG/EM 120–126: α-helix.
127–131: flexible α-helix.
132–143: α-helix.		 [65]
β2 adrenergic receptor turkey IL3 284–295 TMA LPC
TFE
AS		 290–294: α-helix and flexible Nt in LPC; α-helix in TFE; unstructured in AS; random coil in TFE/AS. [67]
human Helix 8 324–357 AS
DMSO
DPC		 SA/MD Unstructured in AS.
α-helix in DMSO and DPC.		 [72]
β1 adrenergic receptor turkey Helix 8 345–359 LMPC
DMPC		 EM α-helix (PDB code:1dep). [73]
AT1A angiotensin receptor rat Helix 8 300–320 AS/TFE SA/MD 306–320: α-helix. [74]
IL2 123–156 TMA DPC-d38 DG/MD 128–139, 147–156: α-helices.
141–145: “U-shape” form.		 [66]
B2 bradykinin receptor rat Ct 309–366 DPC 311–326, 333–345, and 348–363: α-helices. [75]
CB1 cannabinoid receptor human IL3 338–346 AS
AS/Gαi1 		DG Unstructured in AS; α-helix with Gαi1 (PDB code: 1lvq). [68]
IL3 300–343 TMA SDS DG/MD 300–310, 312–319 and 332–346: α-helices.
321–327 and 329–331: turns.		 [124]
Helix 8 397–418 AS
DPC
SDS		 SA/MD Unstructured in AS; α-helix in DPC/SDS. [71]
CB2 cannabinoid receptor human TM1-IL1-TM2 27–101 DMSO Preliminary results [50]
Helix 8 298–319 AS
DMSO
DPC		 SA/MD Unstructured in AS; α-helix in DMSO and DPC. [70]
CCK1 cholecystokini n receptor human Nt
EL3		 1–47, 329–357
352–379		 TMA DPC/AS DG/MD
MD-wd		 1–47: α-helical structures at N- and C-termini and β-sheet stabilized by a disulfide bridge between C18 and C29 (PDB code: 1d6g).
333–337, 341–345, 353–356, 364–367, 372–378: contain helical regions (PDB code: 1hzn).		 [54–56]
CCK2 cholecystokini n receptor human EL3 352–379 TMA DPC/AS DG/MD-wd 332–339, 341–346, and 351–356: contain helical regions (PDB code: 1l4t). [56]
α-Factor receptor (Ste2pR) S. cerevisiae TM6 252–269, C252A TFE/AS DG/EM α-helix with a proline kink. [44]
TM6 252–269, C252A DMPC α-helix with a proline kink (PDB code: 1pjd). [49]
TM7, EL3, Cs 267–339 TFE/AS
CDCl3/CD3
H/AS
LPC
DPC		 DG/SA High helical content of TM7 and Ct in TFE/AS and CDCl3/CD3OH/AS.
Sample stability in detergents was not insufficient for NMR experiments.		 [48]
NK1 Neurokinin receptor rat Ns, EL3 1–39, 264–290 TMA DPC/AS DG/MD-wd 3–10: α-helix.
264–270: α-helix.
276–289: α-helix.		 [58]
EL2 162–198 TMA DPC/AS MD-wd 176–182: α-helix.
187–189: turn.		 [125]
PTH1 parathyroid hormone receptor human Nt 168–198 TMA AS
DPC		 DG/MD Low solubility in AS.
170–174, 178–185, and 189–195: contain α-helical structures.
175–177 and 186–188: contain turns (PDB code: 1bl1.pdb).		 [69]
EL1 241–285 TMA DPC/AS DG/MD-wd 256–264: α-helix.
275–284: three α-helical loops.		 [126]
IL3 382–408 LF, CF2 SDS
AS		 DG 382–393: α-helix with LF and CF2.
394–398: flexible with CF2.
394–406: flexible with LF.
402–408: ordered with CF2.
Unstructured in AS.		 [53]
Rhodopsin bovine TM3-IL2-TM4 125–158 TMA DPC DG/EM 125–137: α-helix.
143–146: turn-like structure.		 [65]
Ct 330–348 AS Unstructured peptide. [33]
Phosphorilated Ct 330–348 AS
AS/arrestin		 DG/MD Unstructured peptide in AS.
The N-terminal portion is flexible and the C-terminal portion assumes a stable helix- loop structure in the presence of arrestin (PDB code: 1nzs).		 [77;78;127]
V1a Vaspressin receptor human IL2 146–166 LF, CF1 AS
TFE/AS		 Random coil conformation in AS; α-helix followed by a β-turn in TFE/AS. [52]
S1P4 Sphingosine 1-phosphate receptor human EL1 95–125 DB
TMA		 AS/TFE DG/MD Partially helical structure (PDB code: 2dco). [61]
NK1 tachykinin receptor TM7 AMSSTM
YNPIISS
L		 DMSO
DMSO/CD
Cl3
PFTB/CD3
OD		 EM/MD Kinked α-helix as a minor conformer in DMSO; increased folded content in DMSO/CDCl3; twoα-helical regions linked by a hinge around the NP motif in PFTB/CD3OD. [45]
A2 tromboxane receptor human EL1 88–104 DB AS DG/MD β-turns. [59]
EL2 173–193 DG/MD A two-turns loop in correspondence of 183 and 188. [60]
IL2–3 129–149, 220–246 DB AS EM/MD IL2: large turn.
IL3: helical-like conformation.		 [51]
a

AS–aqueous solution; BS–biosynthesis in Escherichia coli; CD–circular dichroism; CF1: cyclized form of peptide with termini substituted by S-carboxymethylcysteine; CF2: cyclized form of the peptide with a linker of 8 methylenes; Ct–C-terminus; DB disulfide bridge; DG–distance geometry; DMPC–deuterated dimyristoyl- phosphatidylcholine; DMSO–dimethyl sulfoxide; DPC dodecylphosphocholine micelles; DQF-COSY–double-quantum filtered correlation spectroscopy; EL–extracellular loop EM–energy minimization; HSQC–Heteronuclear single quantum coherence; IL–intracellular loop; LF–linear form of the peptide; LMPC–deuterated lysomyristoyl-phosphatidylcholine; LPC–1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine; MD–molecular dynamics; MD -wd- molecular dynamics in water-decane environment; MS–manual synthesis; NOESY–nuclear overhauser enhancement spectroscopy; Nt–N-terminus; PFTB–perfluoro-tert-butanol; PC–Peptide Constrains; SA–simulated annealing; SDS sodium dodecyl sulfate; SF–solid fase automatic synthesis; ssNMR–solid-state NMR; TFE–trifluoroethanol; TM–transmembrane helix; TMA–transmembrane helix anchor; TOCSY–total correlation spectroscopy; TROSY–transverse relaxation optimized spectroscopy.