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Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail

AutorFlores-Ibarra, Andrea; Vértesy, Sabine; Medrano, Francisco Javier; Gabius, Hans-Joachim; Romero, Antonio
Palabras claveCancer
Structural Biology
Fecha de publicación29-jun-2018
EditorNature Publishing Group
CitaciónScientific reports 8 (1) 9835 (2018)
ResumenAmong members of the family of adhesion/growth-regulatory galectins, galectin-3 (Gal-3) bears a unique modular architecture. A N-terminal tail (NT) consisting of the N-terminal segment (NTS) and nine collagen-like repeatsis linked to the canonical lectin domain. In contrast to bivalent proto- and tandem-repeat-type galectins, Gal-3 is monomeric in solution, capable to self-associate in the presence of bi- to multivalent ligands, and the NTS is involved in cellular compartmentalization. Since no crystallographic information on Gal-3 beyond the lectin domain is available, we used a shortened variant with NTS and repeats VII-IX. This protein crystallized as tetramers with contacts between the lectin domains. The region from Tyr101 (in repeat IX) to Leu114 (in the CRD) formed a hairpin. The NTS extends the canonical beta-sheet of F1-F5 strands with two new beta-strands on the F face. Together, crystallographic and SAXS data reveal a mode of intramolecular structure building involving the highly flexible Gal-3's NT.
Descripción11 p.-8 fig.
Versión del editorhttps://doi.org/10.1038/s41598-018-28235-x
URIhttp://hdl.handle.net/10261/167433
DOI10.1038/s41598-018-28235-x
ISSN2045-2322
E-ISSN2045-2322
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