Homologous Superfamily

Proteinase inhibitor I46, leech metallocarboxypeptidase inhibitor (IPR024063)

Short name: Prot_inh_LCI

Overlapping entries



Leech carboxypeptidase inhibitor (LCI) is a novel protein inhibitor present in the medicinal leech Hirudo medicinalis. The structures of LCI free and bound to carboxypeptidase A2 (CPA2) have been determined by NMR and X-ray crystallography, respectively [PMID: 10742178, PMID: 16126224]. The LCI structure has a motif that comprises a five-stranded antiparallel beta-sheet and one short alpha-helix. This structure is preserved in the complex with human CPA2. The C-terminal tail of LCI becomes rigid upon binding the protease and it interacts with the carboxypeptidase in a substrate-like manner. LCI shares sequence identity at its C terminus (-Thr-Cys-X-Pro-Tyr-Val-X) with carboxypeptidase inhibitors from family I37 - the potato carboxypeptidase inhibitors, this represents a striking example of convergent evolution dictated by the target protease [PMID: 10742178].

Members of this entry belong to the MEROPS inhibitor family I46, clan IS.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.