×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Hemopexin-like domain
Functional Family Matrix metallopeptidase 24

Enzyme Information

3.4.24.80
Membrane-type matrix metalloproteinase-1.
based on mapping to UniProt P50281
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.
-!- Believed to play an important role in the activation of progelatinase A at cell surfaces. -!- Belongs to peptidase family M10.

UniProtKB Entries (1)

P50281
MMP14_HUMAN
Homo sapiens
Matrix metalloproteinase-14

PDB Structure

PDB 2MQS
External Links
Method SOLUTION NMR
Organism
Primary Citation
Transient collagen triple helix binding to a key metalloproteinase in invasion and development.
Zhao, Y., Marcink, T.C., Sanganna Gari, R.R., Marsh, B.P., King, G.M., Stawikowska, R., Fields, G.B., Van Doren, S.R.
Structure
CATH-Gene3D is a Global Biodata Core Resource Learn more...