Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Li, J., Brick, P., O'Hare, M.C., Skarzynski, T., Lloyd, L.F., Curry, V.A., Clark, I.M., Bigg, H.F., Hazleman, B.L., Cawston, T.E., Blow, D.M.(1995) Structure 3: 541-549
- PubMed: 8590015 
- DOI: https://doi.org/10.1016/s0969-2126(01)00188-5
- Primary Citation of Related Structures:  
1FBL - PubMed Abstract: 
The collagenases are members of the family of zinc-dependent enzymes known as the matrix metalloproteinases (MMPs). They are the only proteinases that specifically cleave the collagen triple helix, and are important in a large number of physiological and pathological processes. Structures are known for the N-terminal catalytic' domain of collagenases MMP-1 and MMP-8 and of stromelysin (MMP-3). This catalytic domain alone, which comprises about 150 amino acids, has no activity against collagen. A second domain, of 200 amino acids, is homologous to haemopexin, a haem-binding glycoprotein.
Organizational Affiliation: 
Blackert Laboratory, Imperial College, London, UK.