[HTML][HTML] The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions
A Tochowicz, P Goettig, R Evans, R Visse… - Journal of biological …, 2011 - ASBMB
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 at 1.7 Å resolution. Two interactions were identified
as potential biological dimer interfaces in the crystal structure, and mutagenesis studies
revealed that the biological dimer possesses a symmetrical interaction where blades II and …
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 at 1.7 Å resolution. Two interactions were identified
as potential biological dimer interfaces in the crystal structure, and mutagenesis studies
revealed that the biological dimer possesses a symmetrical interaction where blades II and …