@misc{10481/92132,
year = {2024},
month = {2},
url = {https://hdl.handle.net/10481/92132},
abstract = {Thioredoxins (TRXs) are ubiquitous small, globular proteins involved in cell redox processes. In this work, we
report the solution structure of TRX m from Pisum sativum (pea), which has been determined on the basis of 1444
nuclear Overhauser effect- (NOE-) derived distance constraints. The average pairwise root-mean-square deviation
(RMSD) for the 20 best structures for the backbone residues (Val7-Glu102) was 1.42 ± 0.15 Å, and 1.97 ±
0.15 Å when all heavy atoms were considered. The structure corresponds to the typical fold of TRXs, with a
central five-stranded β-sheet flanked by four α-helices. Some residues had an important exchange dynamic
contribution: those around the active site; at the C terminus of β-strand 3; and in the loop preceding α-helix 4.
Smaller NOE values were observed at the N and C-terminal residues forming the elements of the secondary
structure or, alternatively, in the residues belonging to the loops between those elements. A peptide derived from
pea fructose-1,6-biphosphatase (FBPase), comprising the preceding region to the regulatory sequence of FBPase
(residues Glu152 to Gln179), was bound to TRX m with an affinity in the low micromolar range, as measured by
fluorescence and NMR titration experiments. Upon peptide addition, the intensities of the cross-peaks of all the
residues of TRX m were affected, as shown by NMR. The value of the dissociation constant of the peptide from
TRX m was larger than that of the intact FBPase, indicating that there are additional factors in other regions of
the polypeptide chain of the latter protein affecting the binding to thioredoxin.},
organization = {Consellería de Innovación, Universidades,
Ciencia y Sociedad Digital (Generalitat Valenciana) [CIAICO
2021/0135]},
publisher = {Elsevier},
keywords = {Thioredoxin},
keywords = {Protein-protein interactions},
keywords = {NMR},
title = {Three-dimensional solution structure, dynamics and binding of thioredoxin m from Pisum sativum},
doi = {10.1016/j.ijbiomac.2024.129781},
author = {Neira, José Luis and Palomino Schätzlein, Martina and Rejas, Virginia and Traverso Gutiérrez, José Ángel and Rico, Manual and López Gorgé, Julio and Chueca, Ana and Cámara-Artigas, Ana},
}