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PDBsum entry 2n2f
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Hormone receptor
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PDB id
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2n2f
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PDB id:
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| Name: |
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Hormone receptor
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Title:
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Solution nmr structure of dynorphin 1-13 bound to kappa opioid receptor
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Structure:
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Dynorphin a(1-13). Chain: a. Fragment: residues 207-219. Synonym: proenkephalin-b, beta-neoendorphin-dynorphin, preprodynorphin. Engineered: yes
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Source:
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Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Other_details: synthesis of the peptide was performed by a solid phase method using fmoc chemistry.
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NMR struc:
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10 models
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Authors:
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C.O'Connor,K.White,N.Doncescu,T.Didenko,B.L.Roth,G.Czaplicki, R.C.Stevens,K.Wuthrich,A.Milon
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Key ref:
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C.O'Connor
et al.
(2015).
NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.
Proc Natl Acad Sci U S A,
112,
11852-11857.
PubMed id:
DOI:
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Date:
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06-May-15
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Release date:
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09-Sep-15
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PROCHECK
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Headers
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References
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P01213
(PDYN_HUMAN) -
Proenkephalin-B from Homo sapiens
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Seq:
Struc:
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254 a.a.
13 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Proc Natl Acad Sci U S A
112:11852-11857
(2015)
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PubMed id:
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NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.
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C.O'Connor,
K.L.White,
N.Doncescu,
T.Didenko,
B.L.Roth,
G.Czaplicki,
R.C.Stevens,
K.Wüthrich,
A.Milon.
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ABSTRACT
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The structure of the dynorphin (1-13) peptide (dynorphin) bound to the human
kappa opioid receptor (KOR) has been determined by liquid-state NMR
spectroscopy. (1)H and (15)N chemical shift variations indicated that free and
bound peptide is in fast exchange in solutions containing 1 mM dynorphin and
0.01 mM KOR. Radioligand binding indicated an intermediate-affinity interaction,
with a Kd of ∼200 nM. Transferred nuclear Overhauser enhancement spectroscopy
was used to determine the structure of bound dynorphin. The N-terminal opioid
signature, YGGF, was observed to be flexibly disordered, the central part of the
peptide from L5 to R9 to form a helical turn, and the C-terminal segment from
P10 to K13 to be flexibly disordered in this intermediate-affinity bound state.
Combining molecular modeling with NMR provided an initial framework for
understanding multistep activation of a G protein-coupled receptor by its
cognate peptide ligand.
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