[HTML][HTML] Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed …
CM Overall, AE King, DK Sam, AD Ong, TTY Lau… - Journal of Biological …, 1999 - ASBMB
Cell surface activation of progelatinase A occurs in a quaternary complex with the tissue
inhibitor of metalloproteinases-2 (TIMP-2) and two membrane-type matrix
metalloproteinases. We have mutated the unique cationic clusters found in hemopexin
modules III and IV of the carboxyl domain (C domain) of human gelatinase A to determine
their role in binding TIMP-2. Twelve single, double, and triple site-directed mutations were
produced that exhibited different TIMP-2 binding properties. Notably, single alanine …
inhibitor of metalloproteinases-2 (TIMP-2) and two membrane-type matrix
metalloproteinases. We have mutated the unique cationic clusters found in hemopexin
modules III and IV of the carboxyl domain (C domain) of human gelatinase A to determine
their role in binding TIMP-2. Twelve single, double, and triple site-directed mutations were
produced that exhibited different TIMP-2 binding properties. Notably, single alanine …