1L4Z

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS

1L4Z の概要

• エントリーDOI: 10.2210/pdb1l4z/pdb
• 関連するPDBエントリー: 1BML 1BUI 1DDJ 1L4D 1QRZ
• 分子名称: Plasminogen, Streptokinase, CADMIUM ION, ... (4 entities in total)
• 機能のキーワード: plasminogen, streptokinase, protein complex, hydrolase-blood clotting complex, hydrolase/blood clotting
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P00747
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42759.41

構造登録者

Wakeham, N.,Terzyan, S.,Zhai, P.,Loy, J.A.,Tang, J.,Zhang, X.C. (登録日: 2002-03-06, 公開日: 2002-12-11, 最終更新日: 2024-10-16)

主引用文献

Wakeham, N.,Terzyan, S.,Zhai, P.,Loy, J.A.,Tang, J.,Zhang, X.C.
Effects of deletion of streptokinase residues 48-59 on plasminogen activation.
PROTEIN ENG., 15:753-761, 2002

PubMed Abstract: Streptokinase (SK) is a thrombolytic agent widely used for the clinical treatment of clotting disorders such as heart attack. The treatment is based on the ability of SK to bind plasminogen (Pg) or plasmin (Pm), forming complexes that proteolytically activate other Pg molecules to Pm, which carries out fibrinolysis. SK contains three major domains. The N-terminal domain, SKalpha, provides the complex with substrate recognition towards Pg. SKalpha contains a unique mobile loop, residues 45-70, absent in the corresponding domains of other bacterial Pg activators. To study the roles of this loop, we deleted 12 residues in this loop in both full-length SK and the SKalpha fragment. Kinetic data indicate that this loop participates in the recognition of substrate Pg, but does not function in the active site formation in the activator complex. Two crystal structures of the deletion mutant of SKalpha (SKalpha(delta)) complexed with the protease domain of Pg were determined. While the structure of SKalpha(delta) is essentially the same as this domain in full-length SK, the mode of SK-Pg interaction was however different from a previously observed structure. Even though mutagenesis studies indicated that the current complex represents a minor interacting form in solution, the binding to SKalpha(delta) triggered similar conformational changes in the Pg active site in both crystal forms.

PubMed: 12456874
DOI: 10.1093/protein/15.9.753

実験手法

X-RAY DIFFRACTION (2.8 Å)