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PDBsum entry 1gh2
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Electron transport
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PDB id
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1gh2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the catalytic domain of a human thioredoxin-Like protein.
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Authors
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J.Jin,
X.Chen,
Y.Zhou,
M.Bartlam,
Q.Guo,
Y.Liu,
Y.Sun,
Y.Gao,
S.Ye,
G.Li,
Z.Rao,
B.Qiang,
J.Yuan.
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Ref.
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Eur J Biochem, 2002,
269,
2060-2068.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Fig. 1. Expression pattern of the hTRXL transcript.
Differential expression of hTRXL in human fetal cerebrum of 33-
and 13-weeks-old. Human adult tissue Poly(A^+) RNA Northern blot
(ClonTech). The ^32P-labeled probe is the EST obtained from
DDRT-PCR (GenBank accession no. U48630) and the control used is
 -actin cDNA
(ClonTech).
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Figure 7.
Fig. 7. Molecular surface comparison between hTRX and
hTRXL-N. Molecular surface representations of hTRX (A) and
hTRXL-N (B) around the active surface in the same orientation
were produced using GRASP. Electrostatic surface potentials are
contoured from -30 (red) to 30 (blue) k[b]T·e^-1. The
ellipses highlight the position of active site in hTRX and
hTRXL-N, respectively.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2002,
269,
2060-2068)
copyright 2002.
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