1GH2

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

1GH2 の概要

• エントリーDOI: 10.2210/pdb1gh2/pdb
• 分子名称: THIOREDOXIN-LIKE PROTEIN (2 entities in total)
• 機能のキーワード: redox-active center, electron transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11628.19

構造登録者

Jin, J.,Chen, X.,Guo, Q.,Yuan, J.,Qiang, B.,Rao, Z. (登録日: 2000-11-01, 公開日: 2001-05-01, 最終更新日: 2024-11-13)

主引用文献

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.
Crystal structure of the catalytic domain of a human thioredoxin-like protein.
Eur.J.Biochem., 269:2060-2068, 2002

PubMed Abstract: 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.

PubMed: 11985582
DOI: 10.1046/j.1432-1033.2002.02844.x

実験手法

X-RAY DIFFRACTION (2.22 Å)