1gh2

From Proteopedia

Revision as of 13:53, 15 February 2008

Crystal structure of the catalytic domain of a new human thioredoxin-like protein

Overview

Thioredoxin is a ubiquitous dithiol oxidoreductase found in many organisms, and involved in numerous biochemical processes. Human thioredoxin-like, protein (hTRXL) is differentially expressed at different development, stages of human fetal cerebrum and belongs to an expanding family of, thioredoxins. We have solved the crystal structure of the recombinant, N-terminal catalytic domain (hTRXL-N) of hTRXL in its oxidized form at, 2.2-A resolution. Although this domain shares a similar three-dimensional, structure with human thioredoxin (hTRX), a unique feature of hTRXL-N is, the large number of positively charged residues distributed around the, active site, which has been implicated in substrate specificity., Furthermore, the hTRXL-N crystal structure is monomeric while hTRX is, dimeric in its four crystal structures (reduced, oxidized, C73S and, C32S/C35S mutants) reported to date. As dimerization is the key regulatory, factor in hTRX, the positive charge and lack of dimer formation of hTRXL-N, suggest that it could interact with the acidic amino-acid rich C-terminal, region, thereby suggesting a novel regulation mechanism.

About this Structure

1GH2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of a human thioredoxin-like protein., Jin J, Chen X, Zhou Y, Bartlam M, Guo Q, Liu Y, Sun Y, Gao Y, Ye S, Li G, Rao Z, Qiang B, Yuan J, Eur J Biochem. 2002 Apr;269(8):2060-8. PMID:11985582

Page seeded by OCA on Fri Feb 15 15:53:26 2008