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- PDB-2l27: NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist -

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Basic information

Entry
Database: PDB / ID: 2l27
TitleNMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist
Components
  • Corticotropin-releasing factor receptor 1
  • peptide agonist
KeywordsMEMBRANE PROTEIN / Peptide binding protein / CRF / ECD1 / Agonist / Family B1 / Alpha helical CRF
Function / homology
Function and homology information


regulation of adenylate cyclase activity involved in G protein-coupled receptor signaling pathway / corticotropin-releasing hormone binding / corticotropin-releasing hormone receptor activity / regulation of corticosterone secretion / corticotrophin-releasing factor receptor activity / corticotropin secretion / general adaptation syndrome, behavioral process / parturition / cellular response to corticotropin-releasing hormone stimulus / negative regulation of voltage-gated calcium channel activity ...regulation of adenylate cyclase activity involved in G protein-coupled receptor signaling pathway / corticotropin-releasing hormone binding / corticotropin-releasing hormone receptor activity / regulation of corticosterone secretion / corticotrophin-releasing factor receptor activity / corticotropin secretion / general adaptation syndrome, behavioral process / parturition / cellular response to corticotropin-releasing hormone stimulus / negative regulation of voltage-gated calcium channel activity / behavioral response to ethanol / fear response / G protein-coupled peptide receptor activity / Class B/2 (Secretin family receptors) / exploration behavior / adrenal gland development / activation of adenylate cyclase activity / female pregnancy / adenylate cyclase-activating G protein-coupled receptor signaling pathway / G alpha (s) signalling events / cell surface receptor signaling pathway / endosome / neuron projection / immune response / membrane / plasma membrane
Similarity search - Function
GPCR, family 2, corticotropin releasing factor receptor, type 1 / GPCR, family 2, corticotropin releasing factor receptor / GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily ...GPCR, family 2, corticotropin releasing factor receptor, type 1 / GPCR, family 2, corticotropin releasing factor receptor / GPCR, family 2, extracellular hormone receptor domain / Hormone receptor fold / G-protein coupled receptors family 2 signature 1. / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. / GPCR, family 2, secretin-like, conserved site / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Corticotropin-releasing factor receptor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
Model detailslowest energy, model 1
AuthorsGrace, C.R.R. / Perrin, M.H. / Gulyas, J.R.R. / Rivier, J.E. / Vale, W.W. / Riek, R.R.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: NMR structure of the first extracellular domain of corticotropin-releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist.
Authors: Grace, C.R. / Perrin, M.H. / Gulyas, J. / Rivier, J.E. / Vale, W.W. / Riek, R.
History
DepositionAug 12, 2010Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 1, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 1, 2017Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Corticotropin-releasing factor receptor 1
B: peptide agonist


Theoretical massNumber of molelcules
Total (without water)13,5602
Polymers13,5602
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)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Corticotropin-releasing factor receptor 1 / CRF-R-1 / CRF-R1 / CRFR-1 / Corticotropin-releasing hormone receptor 1 / CRH-R-1 / CRH-R1


Mass: 9278.299 Da / Num. of mol.: 1 / Fragment: residues 28-111
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CRHR1, CRFR, CRFR1, CRHR / Plasmid: pET-32a(+)(Novagen) / Production host: Escherichia coli (E. coli) / References: UniProt: P34998
#2: Protein/peptide peptide agonist


Mass: 4281.854 Da / Num. of mol.: 1 / Source method: obtained synthetically

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D HNCA
1213D HN(CA)CB
1313D 1H-15N NOESY
1413D 1H-13C NOESY
1513D (H)CCH-COSY
1623D HNCA
1723D HN(CA)CB
1823D 1H-15N NOESY
1923D 1H-13C NOESY
11023D (H)CCH-TOCSY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.3 mM [U-100% 13C; U-100% 15N] ECD1-CRF-R1, 90% H2O/10% D2O90% H2O/10% D2O
20.4 mM [U-100% 13C; U-100% 15N] Alpha Helical CRF, 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.3 mMECD1-CRF-R1-1[U-100% 13C; U-100% 15N]1
0.4 mMAlpha Helical CRF-2[U-100% 13C; U-100% 15N]2
Sample conditionsIonic strength: 0.3 / pH: 6.5 / Pressure: ambient / Temperature: 308 K

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NMR measurement

NMR spectrometerType: Bruker INOVA / Manufacturer: Bruker / Model: INOVA / Field strength: 700 MHz

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Processing

NMR software
NameDeveloperClassification
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CYANAGuntert, Mumenthaler and Wuthrichrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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