› 2yx8

X-ray diffraction
2.4Å resolution

Crystal structure of the extracellular domain of human RAMP1

Released:
DOI: 10.2210/pdb2yx8/pdb
PDB entry 2yx8 coloured by chain, front view.
PDB entry 2yx8 coloured by chain, side view.
PDB entry 2yx8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human receptor activity-modifying protein 1 extracellular domain.
Kusano S, Kukimoto-Niino M, Akasaka R, Toyama M, Terada T, Shirouzu M, Shindo T, Yokoyama S
Protein Sci 17 1907-14 (2008)
PMID: 18725456

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor activity-modifying protein 1 Chain: A
Molecule details ›
Chain: A
Length: 93 amino acids
Theoretical weight: 10.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60894 (Residues: 27-112; Coverage: 71%)
Gene name: RAMP1
Sequence domains: Receptor activity modifying family
Structure domains: Receptor activity modifying family

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P4222
Unit cell:
a: 43.097Å b: 43.097Å c: 82.992Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.281
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Calcitonin gene-related peptide: physiology and pathophysiology.
Russell et al. (2014)
9 more

6 mentions without citation

Structure and mechanism for recognition of peptide hormones by Class B G-protein-coupled receptors.
Pal et al. (2012)
5 more