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Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution.

Abstract：

:Eosinophil cationic protein (ECP; RNase 3) is a human ribonuclease found only in eosinophil leukocytes that belongs to the RNase A superfamily. This enzyme is bactericidal, helminthotoxic and cytotoxic to mammalian cells and tissues. The protein has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data up to 1. 75 A resolution. The molecule displays the alpha+beta folding topology typical for members of the ribonuclease A superfamily. The catalytic active site residues are conserved with respect to other ribonucleases of the superfamily but some differences appear at substrate recognition subsites, which may account, in part, for the low catalytic activity. Most strikingly, 19 surface-located arginine residues confer a strong basic character to the protein. The high concentration of positive charges and the particular orientation of the side-chains of these residues may also be related to the low activity of ECP as a ribonuclease and provides an explanation for its unique cytotoxic role through cell membrane disruption.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Mallorquí-Fernández G,Pous J,Peracaula R,Aymamí J,Maeda T,Tada H,Yamada H,Seno M,de Llorens R,Gomis-Rüth FX,Coll M

doi

10.1006/jmbi.2000.3939

keywords:

subject

Has Abstract

pub_date

2000-07-28 00:00:00

pages

1297-307

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)93939-1

journal_volume

300

pub_type

杂志文章

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