1CXW

THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2

Summary for 1CXW

• Entry DOI: 10.2210/pdb1cxw/pdb
• NMR Information: BMRB: 4510
• Descriptor: HUMAN MATRIX METALLOPROTEINASE 2 (1 entity in total)
• Functional Keywords: beta sheet, alpha helix, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P08253
• Total number of polymer chains: 1
• Total formula weight: 6773.36

Authors

Briknarova, K.,Grishaev, A.,Banyai, L.,Tordai, H.,Patthy, L.,Llinas, M. (deposition date: 1999-08-31, release date: 1999-11-12, Last modification date: 2024-10-30)

Primary citation

Briknarova, K.,Grishaev, A.,Banyai, L.,Tordai, H.,Patthy, L.,Llinas, M.
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
Structure Fold.Des., 7:1235-1245, 1999

PubMed Abstract: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type IV collagenase) has an important role in extracellular matrix degradation during cell migration and tissue remodeling. It is involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes. The enzyme cleaves several types of collagen, elastin, fibronectin and laminin. Binding to collagen is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active site.

PubMed: 10545322
DOI: 10.1016/S0969-2126(00)80057-X

Experimental method

SOLUTION NMR