Reck forms cowbell-shaped dimers and inhibits matrix metalloproteinase-catalyzed cleavage of fibronectin*

HIGHLIGHTS

• who: Akira Omura from the , and FN , and is known to be susceptible to some other proteases, including thermolysin, cathepsin D, and chymotrypsin (36)Previous studies using several , substrates, including osteopontin (37), Fas ligand (38, ), type IIA procollagen (40), procryptdins (41, ), and , (43), indicate that cleavage occurs frequently between a polar amino acid (e_g Ser, Gln, Arg, Lys, Asp, and Glu at subsite, ) and a hydrophobic amino acid (e_g Leu, Ile, and Val at subsite P⬘1). The , target site we identified in FN is typical in its P⬘, subsite (Leu) but atypical in its , subsite (Pro . . .
  

   

  

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