The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions.
Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP, a crystal structure of the Hpx domain was solved...
Hauptverfasser: | Tochowicz, A, Goettig, P, Evans, R, Visse, R, Shitomi, Y, Palmisano, R, Ito, N, Richter, K, Maskos, K, Franke, D, Svergun, D, Nagase, H, Bode, W, Itoh, Y |
---|---|
Format: | Journal article |
Sprache: | English |
Veröffentlicht: |
2011
|
Ähnliche Einträge
Ähnliche Einträge
-
Crystal structure of MT1-MMP hemopexin domain: identification of the dimer interface
von: Tochowicz, A, et al.
Veröffentlicht: (2010) -
Distinct roles of the hemopexin and the transmembrane domains as dimer interfaces of MT1-MMP on the cell surface
von: Itoh, Y, et al.
Veröffentlicht: (2007) -
Triple-helical collagen unwinding relies on cooperative binding of the catalytic and hemopexin domains of collagenase
von: Manka, S, et al.
Veröffentlicht: (2010) -
Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
von: Visse, R, et al.
Veröffentlicht: (2003) -
CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase.
von: Suenaga, N, et al.
Veröffentlicht: (2005)