› 4lp5

X-ray diffraction
3.8Å resolution

Crystal structure of the full-length human RAGE extracellular domain (VC1C2 fragment)

Released:
DOI: 10.2210/pdb4lp5/pdb
PDB entry 4lp5 coloured by chain, front view.
PDB entry 4lp5 coloured by chain, side view.
PDB entry 4lp5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the oligomerization mode of the human receptor for advanced glycation end-products.
Yatime L, Andersen GR
FEBS J 280 6556-68 (2013)
PMID: 24119142

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Advanced glycosylation end product-specific receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 32.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15109 (Residues: 23-323; Coverage: 79%)
Gene names: AGER, RAGE
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P65
Unit cell:
a: 180.01Å b: 180.01Å c: 48.95Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.242 0.286
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Targeting RAGE Signaling in Inflammatory Disease.
Hudson et al. (2018)
12 more

10 mentions without citation

Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs.
Twarda-Clapa et al. (2022)
9 more