The crystal structure of the mouse glandular kallikrein‐13 (prorenin converting enzyme)

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Abstract
A crystal structure of the serine protease, mouse glandular kallikrein 13 (mGK‐13) has been determined at 2.6‐Å resolution. This enzyme, isolated from the mouse submandibular gland, is also known as prorenin‐converting enzyme and cleaves submandibular gland Ren‐2 prorenin to yield active renin. The mGK‐13 structure is similar to other members of the mammalian serine protease family, having five conserved disulfide bonds and an active site located in the cleft between two β‐barrel domains. The mGK‐13 structure reveals for the first time an ordered kallikrein loop conformation containing a short 310 helix. This loop is disordered in the related porcine pancreatic kallikrein and rat submandibular tonin structures. The kallikrein loop is in close spatial proximity to the active site and is also involved in a dimeric arrangement of mGK‐13. The catalytic specificity of mCK‐13 for Ren‐2 prorenin was studied by modeling a prorenin‐derived peptide into the active site of mGK‐13. This model emphasizes two electronegative substrate specificity pockets on the mGK‐13 surface, which could accommodate the dibasic P2 and P1 residues at the site of prorenin cleavage by mGK‐13.