› 1t32

X-ray diffraction
1.85Å resolution

A Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase with Therapeutic Efficacy in Animals Models of Inflammation

Released:
DOI: 10.2210/pdb1t32/pdb
PDB entry 1t32 coloured by chain, front view.
PDB entry 1t32 coloured by chain, side view.
PDB entry 1t32 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo.
de Garavilla L, Greco MN, Sukumar N, Chen ZW, Pineda AO, Mathews FS, Di Cera E, Giardino EC, Wells GI, Haertlein BJ, Kauffman JA, Corcoran TW, Derian CK, Eckardt AJ, Damiano BP, Andrade-Gordon P, Maryanoff BE
J Biol Chem 280 18001-7 (2005)
PMID: 15741158

Function and Biology Details

Reaction catalysed: 
Specificity similar to chymotrypsin C.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin G Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.48 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P08311 (Residues: 21-244; Coverage: 95%)
Gene name: CTSG
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand OHH 1 x OHH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 38.8Å b: 62.3Å c: 79.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.213
Expression system: Not provided

Quick links

Citations

16 review citations

Neutrophils and immunity: challenges and opportunities.
Nathan C. (2006)
15 more

2 mentions without citation

Neutrophil elastase reduces secretion of secretory leukoproteinase inhibitor (SLPI) by lung epithelial cells: role of charge of the proteinase-inhibitor complex.
Sullivan et al. (2008)
1 more