› 2rmi

Solution NMR

3D NMR structure of astressin

Released:
DOI: 10.2210/pdb2rmi/pdb
PDB entry 2rmi coloured by chain, ensemble of 20 models, front view.
PDB entry 2rmi coloured by chain, ensemble of 20 models, side view.
PDB entry 2rmi coloured by chain, ensemble of 20 models, top view.
Source organism: Synthetic construct
Primary publication:
Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide.
Grace CR, Cervini L, Gulyas J, Rivier J, Riek R
Biopolymers 87 196-205
PMID: 17657708

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
astressin Chain: A
Molecule details ›
Chain: A
Length: 30 amino acids
Theoretical weight: 3.59 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand DPN 1 x DPN
Ligand NLE 2 x NLE

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided

Quick links

Citations

1 review citation

Corticotropin-releasing factor peptide antagonists: design, characterization and potential clinical relevance.
Rivier et al. (2014)
3 other articles

1 mention without citation

Residues of corticotropin releasing factor-binding protein (CRF-BP) that selectively abrogate binding to CRF but not to urocortin 1.
Huising et al. (2008)