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- PDB-6za8: Crystal structure of the neurotensin receptor 1 in complex with t... -

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Basic information

Entry
Database: PDB / ID: 6za8
TitleCrystal structure of the neurotensin receptor 1 in complex with the small-molecule partial agonist RTI-3a
ComponentsNeurotensin receptor type 1,Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1),Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1)
KeywordsMEMBRANE PROTEIN / GPCR-ligand complex / rNTSR1 / RTI-3a / partial agonist
Function / homology
Function and homology information


Peptide ligand-binding receptors / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / positive regulation of inhibitory postsynaptic potential / symmetric synapse / D-aspartate import across plasma membrane / positive regulation of gamma-aminobutyric acid secretion / L-glutamate import across plasma membrane / positive regulation of arachidonic acid secretion / neuron spine ...Peptide ligand-binding receptors / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / positive regulation of inhibitory postsynaptic potential / symmetric synapse / D-aspartate import across plasma membrane / positive regulation of gamma-aminobutyric acid secretion / L-glutamate import across plasma membrane / positive regulation of arachidonic acid secretion / neuron spine / regulation of respiratory gaseous exchange / negative regulation of release of sequestered calcium ion into cytosol / negative regulation of systemic arterial blood pressure / G alpha (q) signalling events / positive regulation of glutamate secretion / positive regulation of inositol phosphate biosynthetic process / temperature homeostasis / response to lipid / regulation of membrane depolarization / detection of temperature stimulus involved in sensory perception of pain / neuropeptide signaling pathway / axon terminus / adult locomotory behavior / positive regulation of release of sequestered calcium ion into cytosol / dendritic shaft / learning / terminal bouton / cytoplasmic side of plasma membrane / perikaryon / dendritic spine / positive regulation of apoptotic process / membrane raft / axon / neuronal cell body / dendrite / protein-containing complex binding / positive regulation of gene expression / negative regulation of apoptotic process / cell surface / identical protein binding / plasma membrane
Similarity search - Function
Neurotensin receptor / Neurotensin type 1 receptor / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family)
Similarity search - Domain/homology
Chem-SR5 / Neurotensin receptor type 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.72 Å
AuthorsDeluigi, M. / Klipp, A. / Hilge, M. / Merklinger, L. / Klenk, C. / Plueckthun, A.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_182334 Switzerland
CitationJournal: Sci Adv / Year: 2021
Title: Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism.
Authors: Deluigi, M. / Klipp, A. / Klenk, C. / Merklinger, L. / Eberle, S.A. / Morstein, L. / Heine, P. / Mittl, P.R.E. / Ernst, P. / Kamenecka, T.M. / He, Y. / Vacca, S. / Egloff, P. / Honegger, A. / Pluckthun, A.
History
DepositionJun 5, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 10, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 24, 2021Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Mar 17, 2021Group: Database references / Category: citation_author / Item: _citation_author.identifier_ORCID
Revision 1.3Jan 24, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z ..._atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AAA: Neurotensin receptor type 1,Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1),Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6122
Polymers53,0891
Non-polymers5231
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area20440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.468, 211.197, 93.703
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein Neurotensin receptor type 1,Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1),Neurotensin receptor type 1,Neurotensin receptor 1 (NTSR1),Neurotensin receptor 1 (NTSR1) / NTR1 / High-affinity levocabastine-insensitive neurotensin receptor / NTRH


Mass: 53089.223 Da / Num. of mol.: 1
Mutation: S83G,A86L,T101R,H103D,H105Y,L119F,M121L,E124D,R143K,D150E,A161V,R167L,R213L,V234L,K235R,V240L,I253A,I260A,N262R,K263R,H305R,C332V,F342A,T354S,F358V,S362A
Source method: isolated from a genetically manipulated source
Details: Residues 59-371 represent the rat neurotensin receptor 1 mutant H4 (NTSR1-H4). Residues 273 to 290 were deleted for crystallisation purposes. Residues 372 to 380 form a linker connecting ...Details: Residues 59-371 represent the rat neurotensin receptor 1 mutant H4 (NTSR1-H4). Residues 273 to 290 were deleted for crystallisation purposes. Residues 372 to 380 form a linker connecting NTSR1 with the DARPin crystallisation chaperone. Residues 381 to 536 represent the DARPin crystallisation chaperone that is related to 5LW2. Residues 537 to 539 represent a short linker connecting the DARPin crystallisation chaperone with the HRV 3C protease recognition sequence. Residues 540 to 543 are part of the HRV 3C protease recognition sequence visible in the electron density.
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ntsr1, Ntsr / Production host: Escherichia coli (E. coli) / References: UniProt: P20789
#2: Chemical ChemComp-SR5 / (2~{S})-2-[[1-(7-chloranylquinolin-4-yl)-5-(2,6-dimethoxyphenyl)pyrazol-3-yl]carbonylamino]-4-methyl-pentanoic acid


Mass: 522.980 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H27ClN4O5 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.44 Å3/Da / Density % sol: 64.24 %
Crystal growTemperature: 293.1 K / Method: lipidic cubic phase
Details: 100 mM HEPES 385-550 mM Na citrate 30-32% (v/v) PEG400 10 uM RTI-3a
PH range: 6.6 - 7.2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: Y
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.99998 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 11, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99998 Å / Relative weight: 1
ReflectionResolution: 2.72→29.64 Å / Num. obs: 13577 / % possible obs: 90.4 % / Redundancy: 6.5 % / CC1/2: 0.975 / Rmerge(I) obs: 0.259 / Rpim(I) all: 0.106 / Rrim(I) all: 0.281 / Net I/σ(I): 5.2
Reflection shellResolution: 2.72→3.014 Å / Rmerge(I) obs: 2.395 / Num. unique obs: 679 / CC1/2: 0.435 / Rpim(I) all: 0.913 / Rrim(I) all: 2.571
Serial crystallography sample deliveryMethod: fixed target

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Processing

Software
NameVersionClassification
REFMAC5.8.0258refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6YVR

6yvr


Resolution: 2.72→29.64 Å / Cor.coef. Fo:Fc: 0.873 / Cor.coef. Fo:Fc free: 0.867 / WRfactor Rfree: 0.32 / WRfactor Rwork: 0.294 / SU B: 19.486 / SU ML: 0.364 / Average fsc free: 0.8361 / Average fsc work: 0.8489 / Cross valid method: FREE R-VALUE / ESU R Free: 0.489
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.3001 656 4.837 %
Rwork0.2815 12905 -
all0.282 --
obs-13561 65.072 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 50.142 Å2
Baniso -1Baniso -2Baniso -3
1-0.908 Å20 Å20 Å2
2---0.778 Å20 Å2
3----0.13 Å2
Refinement stepCycle: LAST / Resolution: 2.72→29.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3313 0 37 0 3350
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0020.0133439
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173122
X-RAY DIFFRACTIONr_angle_refined_deg1.1651.6164724
X-RAY DIFFRACTIONr_angle_other_deg1.1071.5727122
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.3885448
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.01922.518139
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.27115458
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.991512
X-RAY DIFFRACTIONr_chiral_restr0.0340.2471
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.024053
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02743
X-RAY DIFFRACTIONr_nbd_refined0.1760.2796
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1670.22791
X-RAY DIFFRACTIONr_nbtor_refined0.1540.21712
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.080.21455
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1370.273
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.180.26
X-RAY DIFFRACTIONr_nbd_other0.1690.230
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2440.22
X-RAY DIFFRACTIONr_mcbond_it1.015.7241803
X-RAY DIFFRACTIONr_mcbond_other1.0085.7241800
X-RAY DIFFRACTIONr_mcangle_it1.8148.5812247
X-RAY DIFFRACTIONr_mcangle_other1.8148.5812248
X-RAY DIFFRACTIONr_scbond_it0.7455.6631636
X-RAY DIFFRACTIONr_scbond_other0.7445.6631637
X-RAY DIFFRACTIONr_scangle_it1.3728.4842477
X-RAY DIFFRACTIONr_scangle_other1.3728.4842478
X-RAY DIFFRACTIONr_lrange_it5.045106.30714477
X-RAY DIFFRACTIONr_lrange_other5.044106.30414478
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.72-2.7910.72730.46747X-RAY DIFFRACTION3.3091
2.791-2.8670.2690.401140X-RAY DIFFRACTION10.0676
2.867-2.950.452130.4234X-RAY DIFFRACTION16.9876
2.95-3.0410.35170.35346X-RAY DIFFRACTION25.2504
3.041-3.140.443240.365426X-RAY DIFFRACTION33.7584
3.14-3.2510.306370.34650X-RAY DIFFRACTION51.4992
3.251-3.3730.393470.333780X-RAY DIFFRACTION65.8439
3.373-3.5110.361450.3181000X-RAY DIFFRACTION85.3061
3.511-3.6670.272530.3071113X-RAY DIFFRACTION98.8974
3.667-3.8450.287580.2861061X-RAY DIFFRACTION99.4667
3.845-4.0530.307550.2751026X-RAY DIFFRACTION99.2654
4.053-4.2990.273410.265970X-RAY DIFFRACTION99.7041
4.299-4.5950.285450.247906X-RAY DIFFRACTION99.895
4.595-4.9620.289420.258850X-RAY DIFFRACTION99.6648
4.962-5.4350.41430.278793X-RAY DIFFRACTION98.9349
5.435-6.0740.279400.332709X-RAY DIFFRACTION99.2053
6.074-7.010.279310.318637X-RAY DIFFRACTION98.6706
7.01-8.5760.302300.236540X-RAY DIFFRACTION98.7868
8.576-12.0880.188200.192437X-RAY DIFFRACTION99.3478
12.088-29.640.268130.345240X-RAY DIFFRACTION90.3571

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