1DTV

NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)

1DTV の概要

• エントリーDOI: 10.2210/pdb1dtv/pdb
• 分子名称: CARBOXYPEPTIDASE INHIBITOR (1 entity in total)
• 機能のキーワード: leech carboxypeptidase inhibitor, lci, hydrolase inhibitor
• 由来する生物種: Hirudo medicinalis (medicinal leech)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7397.26

構造登録者

Reverter, D.,Fernandez-Catalan, C.,Bode, W.,Holak, T.A.,Aviles, F.X. (登録日: 2000-01-13, 公開日: 2000-07-19, 最終更新日: 2024-10-30)

主引用文献

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

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: 10742178
DOI: 10.1038/74092

実験手法

SOLUTION NMR