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1 UPPEER ORO doi: /nature10753 D D D D P E ntracellular C1 W P P C EC1 D Q R H C D W D R C C2 D E D E C R Q Q W P W W R P P EC2 EC3 P C C P W P W W P C W H R C R E C3 P R R P P P C Extracellular embrane H R C H Bound [ 3 H]QB (p) ree [ 3 H]QB (n) 4 lysozyme Bound [ 3 H]QB (%) log [igand] () upplementary igure 1. chematic diagram of the 2-4 and characterization of ligand binding. a, our -linked glycosylation sites in the - terminus were eliminated by converting asparagine residues (sn2, 3, 6 and 9) to aspartic acid (D). he cysteine-less 4 (green) was inserted in the third intracellular loop. b and c, igand binding studies on the 2 (black symbols) and 2-4 (red symbols) receptors. b, aturation binding was assayed by incubating solubilized f9 cellular membranes with n [ 3 H]QB with or without 1 µ atropine. he result of a representative experiment performed three times is shown. he specific activity of [ 3 H]QB was 82 dpm/fmol, the reaction volume was 0.2 ml, and the amount of total membrane protein used was 2.64 µg ( 2 ) and 4.72 µg ( 2-4). Data were fit by curves derived from the assumption of a simple mass action giving d values of 0.31 n ( 2 ) and 0.35 n ( 2-4)
2 REERCH UPPEER ORO in the experiment shown here. aximal binding capacity was estimated to be 155 p ( 2 ) and 168 p ( 2-4), which correspond to 2540 and 2760 dpm/assay tube, 31.0 and 33.6 fmol/0.2 ml, and 11.7 and 7.1 pmol/mg of membrane protein, respectively. c, Displacement of [ 3 H]QB binding by carbamylcholine (circle) or atropine (square). i values for carbamylcholine or atropine were estimated from their concentrations (C 50 ) giving a half maximal inhibition of [ 3 H]QB binding according to the equation i = C 50 /(1 + [[ 3 H]QB]/d*), where d* is the dissociation constant for [ 3 H]QB binding. he concentration of [ 3 H]QB was 2 n. i values for carbamylcholine and atropine were estimated to be 0.14 m and 2.7 n for 2 and 0.17 m and 3.0 n for 2-4, respectively, in the experiment shown here. 2
3 UPPEER ORO REERCH upplementary igure 2. attice packing in the 2-4 crystals. he 2 receptor is shown in blue and 4 lysozyme is shown in red. W W W. U R E. C O / U R E 3
4 REERCH UPPEER ORO upplementary igure 3. Comparison of the 2 receptor structure with other monoamine PCRs. he 2 receptor is shown in blue with the ligand QB in yellow sticks (red for oxygen atoms, blue for nitrogens). Other receptors are shown in grey, with ligands in grey sticks. 4 W W W. U R E. C O / U R E
5 UPPEER ORO REERCH upplementary igure 4. queous channels in structures of protein coupled receptors. Each receptor is colored differently for clarity. he aqueous region passing though much of the 2 receptor is lined by allosteric site and orthosteric site residues, and is additionally bounded below by 65, 68 D69, 72, 106, 110, 114, 392, 396, W400, 430, 432, 433,
6 REERCH UPPEER ORO upplementary igure 5 Electron density in the ligand binding pocket. n o - c ligand omit map is contoured at 3 σ in grey in panels a and b, while panel c also shows a 2 o - c map in green for binding pocket residues contoured at 1.5 σ. 6
7 UPPEER ORO REERCH 250 kda 150 kda 100 kda 75 kda 50 kda 37 kda upplementary igure 6 D-PE and EC analysis of 2-4. he receptor appears to aggregate in the presence of D, accounting for higher molecular weight bands on a gel (left). ize exclusion analysis (right) is a non-denaturing technique, and receptor appears monodisperse by this assay. 7
8 REERCH UPPEER ORO upplementary igure 7 Crystals of 2-4 shown under partially crossed polarizing filters. Crystals were typically 20 microns in the longest dimension, as shown here, although in some cases larger crystals were seen. 8
9 UPPEER ORO REERCH upplementary able 1. he residues in the QB binding sites of 2 R and these equivalents in other aminergenic receptors (1). 2 (2) 1, 3-5 H 1, 2 α 1-D α 2-C β 1-3 D1,5 D2-4 Helix D D D D D D D D / /C C C C Helix W W / / EC2 181 EC2 /Q / // / Helix / / / / /D Helix W W W W W W W W Helix / C C W 1) bbreviations of the receptors are as follows. 2 : muscarinic 2 acetylcholine receptor, 1, 3-5 : muscarinic 1, 3-5 acetylcholine receptors, H 1, 2 : histamine H 1, 2 receptors, α 1-D : α 1-D -adrenergic receptors, α 2-C : α 2-C -adrenergic receptors, β 1-3 : β 1-3 -adrenergic receptors, D1,5: dopamine D1, 5 receptors, D2-4: dopamine D2-4 receptors. 2) uperscripts indicate Ballesteros Weinstein numbering for conserved PCR residues
10 REERCH UPPEER ORO upplementary able 2. Data collection and refinement statistics. Data collection a umber of crystals 23 pace group P 2 1 Cell dimensions a, b, c (Å) 78.2, 47.3, 88.1 α, β, γ ( ) 90.0, 109.7, 90.0 Resolution (Å) ( ) R merge (%) 18.5 (45.4) <>/<σ> 6.1 (1.4) Completeness (%) 94.1 (79.2) Redundancy 3.5 (2.4) Refinement Resolution (Å) o. unique reflections (593 in test set) R work /R free (%) 22.7 / 27.6 nisotropic B tensor B 11 = 18.2 / B 22 = 2.6 / B 33 = / B 13 = 9.8 verage B-factors (Å 2 ) 2 muscarinic receptor 53.3 (R)-( )-3-QB lysozyme 57.8 olvent 42.8 R.m.s. deviation from ideality Bond length (Å) Bond angles ( ) 0.57 Ramachandran statistics b avored regions (%) 98.8 llowed regions (%) 1.2 Outliers (%) 0 a Highest shell statistics are in parentheses. b s defined by olprobity
11 UPPEER ORO REERCH upplementary able 3. elect contacts between QB and 2 receptor QB 2 receptor Distance (Å) a mine sp103 carboxylate 3.3 Carbonyl sn404 H Hydroxyl sn404 carbonyl 2.7 Quinuclidine cage yr426 phenyl 3.9 Quinuclidine cage yr403 phenyl 3.9 Quinuclidine cage yr430 phenyl 3.8 Quinuclidine cage yr104 phenyl 3.6 Quinuclidine cage rp400 indole 4.0 Pro-R phenyl hr187 Cγ 3.9 Pro-R phenyl Phe181 phenyl 3.7 Pro- phenyl yr104 phenyl 4.3 Pro- phenyl la194 Cβ 3.9 Pro- phenyl er107 Cβ 3.9 Pro- phenyl rp155 indole 3.7 a Distances reported are the closest contact between any side chain atom and any ligand atom in the indicated functional groups. b n this structure, the pro-r phenyl ring is positioned closer to the extracellular surface, while the pro- phenyl points toward the cytoplasmic side. iterature Cited 1. Ballesteros, J.. & Weinstein, H. ntegrated methods for the construction of three-dimensional models and computational probing of structurefunction relations in protein coupled receptors. eth. eurosci. 25, (1995). 2. Chen,. B. et al. olprobity: all-atom structure validation for macromolecular crystallography. cta Crystallogr. D Biol. Crystallogr. 66, 12-21, (2010). 11
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