2j3n

From Proteopedia

Revision as of 10:33, 30 October 2007

X-RAY STRUCTURE OF HUMAN THIOREDOXIN REDUCTASE 1

Overview

Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein, crucially involved in the regulation of cellular redox reactions, growth, and differentiation. The enzyme contains a selenocysteine residue at its, C-terminal active site that is essential for catalysis. This redox center, is located on a flexible arm, solvent-exposed and reactive towards, electrophilic inhibitors, thus representing a target for antitumor drug, development. During catalysis reducing equivalents are transferred from, the cofactor NADPH to FAD, then to the N-terminal active site cysteine, residues and from there to the flexible C-terminal part of the other, subunit to be finally delivered to a variety of second substrates at the, molecule's surface. Here we report the first crystal structure of hTrxR1, ... [(full description)]

About this Structure

2J3N is a [Single protein] structure of sequence from [Homo sapiens] with FAD, NAP and MPD as [ligands]. Active as [Thioredoxin-disulfide reductase], with EC number [1.8.1.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis., Fritz-Wolf K, Urig S, Becker K, J Mol Biol. 2007 Jun 29;370(1):116-27. Epub 2007 Apr 24. PMID:17512005

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