1FBL

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

Summary for 1FBL

• Entry DOI: 10.2210/pdb1fbl/pdb
• Descriptor: FIBROBLAST (INTERSTITIAL) COLLAGENASE (MMP-1), CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: metalloprotease
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): P21692
• Total number of polymer chains: 1
• Total formula weight: 43358.94

Authors

Li, J.,Brick, P.,Blow, D.M. (deposition date: 1995-04-24, release date: 1996-01-29, Last modification date: 2024-11-13)

Primary citation

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.
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Structure, 3:541-549, 1995

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.

PubMed: 8590015
DOI: 10.1016/S0969-2126(01)00188-5

Experimental method

X-RAY DIFFRACTION (2.5 Å)