1CG2

CARBOXYPEPTIDASE G2

1CG2 の概要

• エントリーDOI: 10.2210/pdb1cg2/pdb
• 分子名称: CARBOXYPEPTIDASE G2, ZINC ION (3 entities in total)
• 機能のキーワード: metallocarboxypeptidase, hydrolase
• 由来する生物種: Pseudomonas sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 167843.75

構造登録者

Rowsell, S.,Pauptit, R.A.,Tucker, A.D.,Melton, R.G.,Blow, D.M.,Brick, P. (登録日: 1996-12-20, 公開日: 1997-12-24, 最終更新日: 2024-02-14)

主引用文献

Rowsell, S.,Pauptit, R.A.,Tucker, A.D.,Melton, R.G.,Blow, D.M.,Brick, P.
Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy.
Structure, 5:337-347, 1997

PubMed Abstract: Carboxypeptidase G enzymes hydrolyze the C-terminal glutamate moiety from folic acid and its analogues, such as methotrexate. The enzyme studied here, carboxypeptidase G2 (CPG2), is a dimeric zinc-dependent exopeptidase produced by Pseudomonas sp. strain RS-16. CPG2 has applications in cancer therapy: following its administration as an immunoconjugate, in which CPG2 is linked to an antibody to a tumour-specific antigen, it can enzymatically convert subsequently administered inactive prodrugs to cytotoxic drugs selectively at the tumour site. CPG2 has no significant amino acid sequence homology with proteins of known structure. Hence, structure determination of CPG2 was undertaken to identify active-site residues, which may in turn provide ideas for protein and/or substrate modification with a view to improving its therapeutic usefulness.

PubMed: 9083113
DOI: 10.1016/S0969-2126(97)00191-3

実験手法

X-RAY DIFFRACTION (2.5 Å)