› 2ksb

Solution NMR

Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles as a ligand for NK1R

Released:
DOI: 10.2210/pdb2ksb/pdb
PDB 2ksb coloured by chain and viewed from the front.
PDB 2ksb coloured by chain and viewed from the side.
PDB 2ksb coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles.
Gayen A, Goswami SK, Mukhopadhyay C
Biochim Biophys Acta 1808 127-39 (2011)
PMID: 20937248

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Substance-P receptor Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 41.68 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P25103 (Residues: 1-364; Coverage: 89%)
Gene names: NK1R, TAC1R, TACR1
Sequence domains: 7 transmembrane receptor (rhodopsin family)
Structure domains: Rhodopsin 7-helix transmembrane proteins
Substance P Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20366 (Residues: 58-68; Coverage: 10%)
Gene names: NKA, NKNA, TAC1, TAC2
Sequence domains: Tachykinin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 1%
Refinement method: molecular dynamics, simulated annealing
Chemical shifts: BMR20117  
Expression system: Not provided

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Citations

1 review citation

The magic of bicelles lights up membrane protein structure.
Dürr et al. (2012)
16 other articles