1QMT

Recombinant Human Eosinophil Cationic Protein

1QMT の概要

• エントリーDOI: 10.2210/pdb1qmt/pdb
• 分子名称: EOSINOPHIL CATIONIC PROTEIN (2 entities in total)
• 機能のキーワード: eosinophil, ribonuclease, cytotoxicity
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasmic granule: P12724
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15730.07

構造登録者

Boix, E.,Leonidas, D.D.,Acharya, K.R. (登録日: 1999-10-06, 公開日: 2000-02-04, 最終更新日: 2024-11-20)

主引用文献

Boix, E.,Leonidas, D.D.,Nikolovski, Z.,Nogues, M.V.,Cuchillo, C.M.,Acharya, K.R.
The Crystal Structure of Eosinophil Cationic Protein at 2.4 A Resolution
Biochemistry, 38:16794-, 1999

PubMed Abstract: Eosinophil cationic protein (ECP) is located in the matrix of the eosinophil's large specific granule and has marked toxicity for a variety of helminth parasites, hemoflagellates, bacteria, single-stranded RNA virus, and mammalian cells and tissues. It belongs to the bovine pancreatic ribonuclease A (RNase A) family and exhibits ribonucleolytic activity which is about 100-fold lower than that of a related eosinophil ribonuclease, the eosinophil-derived neurotoxin (EDN). The crystal structure of human ECP, determined at 2.4 A, is similar to that of RNase A and EDN. It reveals that residues Gln-14, His-15, Lys-38, Thr-42, and His-128 at the active site are conserved as in all other RNase A homologues. Nevertheless, evidence for considerable divergence of ECP is also implicit in the structure. Amino acid residues Arg-7, Trp-10, Asn-39, His-64, and His-82 appear to play a key part in the substrate specificity and low catalytic activity of ECP. The structure also shows how the cationic residues are distributed on the surface of the ECP molecule that may have implications for an understanding of the cytotoxicity of this enzyme.

PubMed: 10606511
DOI: 10.1021/BI9919145

実験手法

X-RAY DIFFRACTION (2.4 Å)