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- PDB-2lnl: Structure of human CXCR1 in phospholipid bilayers -

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Basic information

Entry
Database: PDB / ID: 2lnl
TitleStructure of human CXCR1 in phospholipid bilayers
ComponentsC-X-C chemokine receptor type 1
KeywordsSIGNALING PROTEIN / G protein coupled receptor / GPCR / chemokine / membrane protein / transmembrane / 7TM / phospholipid / signaling
Function / homology
Function and homology information


interleukin-8 receptor activity / interleukin-8 binding / chemokine receptor activity / C-C chemokine receptor activity / C-C chemokine binding / Chemokine receptors bind chemokines / dendritic cell chemotaxis / neutrophil chemotaxis / secretory granule membrane / G protein-coupled receptor activity ...interleukin-8 receptor activity / interleukin-8 binding / chemokine receptor activity / C-C chemokine receptor activity / C-C chemokine binding / Chemokine receptors bind chemokines / dendritic cell chemotaxis / neutrophil chemotaxis / secretory granule membrane / G protein-coupled receptor activity / calcium-mediated signaling / receptor internalization / positive regulation of cytosolic calcium ion concentration / G alpha (i) signalling events / cell surface receptor signaling pathway / immune response / G protein-coupled receptor signaling pathway / external side of plasma membrane / Neutrophil degranulation / plasma membrane
Similarity search - Function
CXC chemokine receptor 1 / CXC chemokine receptor 1/2 / Rhopdopsin 7-helix transmembrane proteins / Rhodopsin 7-helix transmembrane proteins / 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) / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
C-X-C chemokine receptor type 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLID-STATE NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsPark, S. / Das, B.B. / Casagrande, F. / Nothnagel, H. / Chu, M. / Kiefer, H. / Maier, K. / De Angelis, A. / Marassi, F.M. / Opella, S.J.
CitationJournal: Nature / Year: 2012
Title: Structure of the chemokine receptor CXCR1 in phospholipid bilayers.
Authors: Park, S.H. / Das, B.B. / Casagrande, F. / Tian, Y. / Nothnagel, H.J. / Chu, M. / Kiefer, H. / Maier, K. / De Angelis, A.A. / Marassi, F.M. / Opella, S.J.
History
DepositionDec 31, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Oct 17, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 5, 2012Group: Database references
Revision 1.2Apr 27, 2016Group: Structure summary

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: C-X-C chemokine receptor type 1


Theoretical massNumber of molelcules
Total (without water)35,1611
Polymers35,1611
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein C-X-C chemokine receptor type 1 / CXC-R1 / CXCR-1 / CDw128a / High affinity interleukin-8 receptor A / IL-8R A / IL-8 receptor type 1


Mass: 35161.004 Da / Num. of mol.: 1 / Fragment: UNP residues 20-328
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CMKAR1, CXCR1, IL8RA / Production host: Escherichia coli (E. coli) / References: UniProt: P25024

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NCACX
121SLF
131PDSD

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Sample preparation

DetailsContents: 2-4 mg [U-100% 13C; U-100% 15N] CXCR1, 100% H2O / Solvent system: 100% H2O
SampleUnits: mg/mL / Component: CXCR1-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] / Conc. range: 2-4
Sample conditionsIonic strength: 20 / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 750 MHz

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Processing

NMR softwareName: X-PLOR_NIH / Developer: Schwieters, Kuszewski, Tjandra and Clore / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: THE ANI COORDINATES HAVE BEEN INCLUDED IN THE RESTRAINT FILE. THE ANI Z AXIS SPECIFIES THE DIRECTION OF THE NORMAL TO THE PLANE OF THE LIPID BILAYER MEMBRANE.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 10

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