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

Abstract Among 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 repeats is linked to the canonical lectin domain. In contrast to bivalent pro...

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Autores principales:	Andrea Flores-Ibarra, Sabine Vértesy, Francisco J. Medrano, Hans-Joachim Gabius, Antonio Romero
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2c7acd4b69ae4cc98caad13f41be21b1
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spelling	oai:doaj.org-article:2c7acd4b69ae4cc98caad13f41be21b12021-12-02T15:08:23ZCrystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail10.1038/s41598-018-28235-x2045-2322https://doaj.org/article/2c7acd4b69ae4cc98caad13f41be21b12018-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-28235-xhttps://doaj.org/toc/2045-2322Abstract Among 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 repeats is 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 β-sheet of F1-F5 strands with two new β-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.Andrea Flores-IbarraSabine VértesyFrancisco J. MedranoHans-Joachim GabiusAntonio RomeroNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrea Flores-Ibarra Sabine Vértesy Francisco J. Medrano Hans-Joachim Gabius Antonio Romero Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
description	Abstract Among 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 repeats is 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 β-sheet of F1-F5 strands with two new β-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.
format	article
author	Andrea Flores-Ibarra Sabine Vértesy Francisco J. Medrano Hans-Joachim Gabius Antonio Romero
author_facet	Andrea Flores-Ibarra Sabine Vértesy Francisco J. Medrano Hans-Joachim Gabius Antonio Romero
author_sort	Andrea Flores-Ibarra
title	Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
title_short	Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
title_full	Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
title_fullStr	Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
title_full_unstemmed	Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail
title_sort	crystallization of a human galectin-3 variant with two ordered segments in the shortened n-terminal tail
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/2c7acd4b69ae4cc98caad13f41be21b1
work_keys_str_mv	AT andreafloresibarra crystallizationofahumangalectin3variantwithtwoorderedsegmentsintheshortenednterminaltail AT sabinevertesy crystallizationofahumangalectin3variantwithtwoorderedsegmentsintheshortenednterminaltail AT franciscojmedrano crystallizationofahumangalectin3variantwithtwoorderedsegmentsintheshortenednterminaltail AT hansjoachimgabius crystallizationofahumangalectin3variantwithtwoorderedsegmentsintheshortenednterminaltail AT antonioromero crystallizationofahumangalectin3variantwithtwoorderedsegmentsintheshortenednterminaltail
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Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail

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