2mqs

Solution NMR

Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and Development: Spin Labels to Structure

Released:

Function and Biology Details

Reaction catalysed:
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-156157 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Matrix metalloproteinase-14 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50281 (Residues: 316-511; Coverage: 35%)
Gene name: MMP14
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain
THP_L_and_M_chain Chains: B, C
Molecule details ›
Chains: B, C
Length: 36 amino acids
Theoretical weight: 3.29 KDa
Source organism: Homo sapiens
Expression system: Not provided
THP_T_chain Chain: D
Molecule details ›
Chain: D
Length: 33 amino acids
Theoretical weight: 3.03 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 26%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided