› 2fv9

X-ray diffraction
2.02Å resolution

Crystal structure of TACE in complex with JMV 390-1

Released:
DOI: 10.2210/pdb2fv9/pdb
PDB entry 2fv9 coloured by chain, front view.
PDB entry 2fv9 coloured by chain, side view.
PDB entry 2fv9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stabilization of the autoproteolysis of TNF-alpha converting enzyme (TACE) results in a novel crystal form suitable for structure-based drug design studies.
Ingram RN, Orth P, Strickland CL, Le HV, Madison V, Beyer BM
Protein Eng Des Sel 19 155-61 (2006)
PMID: 16459338

Function and Biology Details

Reaction catalysed: 
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disintegrin and metalloproteinase domain-containing protein 17 Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 29.12 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P78536 (Residues: 218-475; Coverage: 32%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12B Reprolysin-like
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand INN 1 x INN
Ligand 002 1 x 002
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 73.799Å b: 76.221Å c: 102.092Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.251 0.264
Expression system: Trichoplusia ni

Quick links

Citations

4 review citations

The canonical Notch signaling pathway: unfolding the activation mechanism.
Kopan et al. (2009)
3 more

3 mentions without citation

ACE2 (Angiotensin-Converting Enzyme 2) in Cardiopulmonary Diseases: Ramifications for the Control of SARS-CoV-2.
Sharma et al. (2020)
2 more