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spinqualitylabelsall models 1dyt, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY CRYSTAL STRUCTURE OF ECP (RNASE 3) AT 1.75 A

Overview

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.

About this Structure

1DYT is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution., Mallorqui-Fernandez G, Pous J, Peracaula R, Aymami J, Maeda T, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M, J Mol Biol. 2000 Jul 28;300(5):1297-307. PMID:10903870

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