Two-domain aminopeptidase of M1 family: Structural features for substrate binding and gating in absence of C-terminal domain

Volume: 208, Issue: 1, Pages: 51 - 60
Published: Oct 1, 2019
Abstract
Zinc metallopeptidases of the M1 family (M1 peptidases) with unique metal binding motif HEXXH(X)18E regulate many important biological processes such as tumor growth, angiogenesis, hormone regulation, and immune cell development. Typically, these enzymes exist in three-domain [N-terminal domain (N-domain), catalytic domain, and C-terminal domain (C-domain)] or four-domain (N-domain, catalytic domain, middle domain, and C-domain) format in which...
Paper Details
Title
Two-domain aminopeptidase of M1 family: Structural features for substrate binding and gating in absence of C-terminal domain
Published Date
Oct 1, 2019
Volume
208
Issue
1
Pages
51 - 60
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