› 3vlg

X-ray diffraction
2.3Å resolution

Crystal structure of the W150A mutant LOX-1 CTLD showing impaired OxLDL binding

Released:
DOI: 10.2210/pdb3vlg/pdb
PDB entry 3vlg coloured by chain, front view.
PDB entry 3vlg coloured by chain, side view.
PDB entry 3vlg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural implication for the impaired binding of W150A mutant LOX-1 to oxidized low density lipoprotein, OxLDL.
Nakano S, Sugihara M, Yamada R, Katayanagi K, Tate S
Biochim Biophys Acta 1824 739-49 (2012)
PMID: 22369967

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-160259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxidized low-density lipoprotein receptor 1 Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P78380 (Residues: 133-273; Coverage: 52%)
Gene names: CLEC8A, LOX1, OLR1
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P41212
Unit cell:
a: 62.244Å b: 62.244Å c: 76.671Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.246
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Simulative and experimental investigation on the cleavage site that generates the soluble human LOX-1.
Biocca et al. (2013)
3 more

1 mention without citation

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