1DTV
NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)
Summary for 1DTV
| Entry DOI | 10.2210/pdb1dtv/pdb |
| Descriptor | CARBOXYPEPTIDASE INHIBITOR (1 entity in total) |
| Functional Keywords | leech carboxypeptidase inhibitor, lci, hydrolase inhibitor |
| Biological source | Hirudo medicinalis (medicinal leech) |
| Total number of polymer chains | 1 |
| Total formula weight | 7397.26 |
| Authors | Reverter, D.,Fernandez-Catalan, C.,Bode, W.,Holak, T.A.,Aviles, F.X. (deposition date: 2000-01-13, release date: 2000-07-19, Last modification date: 2024-10-30) |
| Primary citation | Reverter, D.,Fernandez-Catalan, C.,Baumgartner, R.,Pfander, R.,Huber, R.,Bode, W.,Vendrell, J.,Holak, T.A.,Aviles, F.X. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nat.Struct.Biol., 7:322-328, 2000 Cited by PubMed Abstract: 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. The LCI structure defines a new protein motif that comprises a five-stranded antiparallel beta-sheet and one short alpha-helix. This structure is preserved in the complex with human CPA2 in the X-ray structure, where the contact regions between the inhibitor and the protease are defined. The C-terminal tail of LCI becomes rigid upon binding the protease as shown in the NMR relaxation studies, and it interacts with the carboxypeptidase in a substrate-like manner. The homology between the C-terminal tails of LCI and the potato carboxypeptidase inhibitor represents a striking example of convergent evolution dictated by the target protease. These new structures are of biotechnological interest since they could elucidate the control mechanism of metallo-carboxypeptidases and could be used as lead compounds for the search of fibrinolytic drugs. PubMed: 10742178DOI: 10.1038/74092 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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