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spinqualitylabelsall models 1wdy, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of ribonuclease

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

An interferon-induced endoribonuclease, ribonuclease L (RNase L), is, implicated in both the molecular mechanism of action of interferon and the, fundamental control of RNA stability in mammalian cells. RNase L is, catalytically active only after binding to an unusual activator molecule, containing a 5'-phosphorylated 2',5'-linked oligoadenylate (2-5A), in the, N-terminal half. Here, we report the crystal structure of the N-terminal, ankyrin repeat domain (ANK) of human RNase L complexed with the activator, 2-5A. This is the first structural view of an ankyrin repeat structure, directly interacting with a nucleic acid, rather than with a protein. The, ANK domain folds into eight ankyrin repeat elements and forms an extended, curved structure with a concave surface. The 2-5A molecule is accommodated, at a concave site and directly interacts with ankyrin repeats 2-4., Interestingly, two structurally equivalent 2-5A binding motifs are found, at repeats 2 and 4. The structural basis for 2-5A recognition by ANK is, essential for designing stable 2-5As with a high likelihood of activating, RNase L.

Disease

Known diseases associated with this structure: Prostate cancer 1, 176807 OMIM:[180435]

About this Structure

1WDY is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L., Tanaka N, Nakanishi M, Kusakabe Y, Goto Y, Kitade Y, Nakamura KT, EMBO J. 2004 Oct 13;23(20):3929-38. Epub 2004 Sep 23. PMID:15385955

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