2PK4

THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE

2PK4 の概要

• エントリーDOI: 10.2210/pdb2pk4/pdb
• 分子名称: HUMAN PLASMINOGEN KRINGLE 4, 6-AMINOHEXANOIC ACID (3 entities in total)
• 機能のキーワード: hydrolase(serine protease)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted : P00747
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9300.28

構造登録者

Tulinsky, A.,Wu, T.-P. (登録日: 1991-07-18, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Wu, T.P.,Padmanabhan, K.,Tulinsky, A.,Mulichak, A.M.
The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4.
Biochemistry, 30:10589-10594, 1991

PubMed Abstract: The crystallographic structure of the plasminogen kringle 4-epsilon-aminocaproic acid (ACA) complex (K4-ACA) has been solved by molecular replacement rotation-translation methods utilizing the refined apo-K4 structure as a search model (Mulichak et al., 1991), and it has been refined to an R value of 0.148 at 2.25-A resolution. The K4-ACA structure consists of two interkringle residues, the kringle along with the ACA ligand, and 106 water molecules. The lysine-binding site has been confirmed to be a relatively open and shallow depression, lined by aromatic rings of Trp62, Phe64, and Trp72, which provide a highly nonpolar environment between doubly charged anionic and cationic centers formed by Asp55/Asp57 and Lys35/Arg71. A zwitterionic ACA ligand molecule is held by hydrogen-bonded ion pair interactions and van der Waals contacts between the charged centers. The lysine-binding site of apo-K4 and K4-ACA have been compared: the rms differences in main-chain and side-chain positions are 0.25 and 0.69 A, respectively, both practically within error of the determinations. The largest deviations in the binding site are due to different crystal packing interactions. Thus, the lysine-binding site appears to be preformed, and lysine binding does not require conformational changes of the host. The results of NMR studies of lysine binding with K4 are correlated with the structure of K4-ACA and agree well.

PubMed: 1657149
DOI: 10.1021/bi00107a030

実験手法

X-RAY DIFFRACTION (2.25 Å)