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Preliminary X‐ray crystallographic analysis of an engineered variant of human chimera‐type galectin‐3 with a shortened N‐terminal domain
Author(s) -
FloresIbarra Andrea,
Ruiz Federico M.,
Vértesy Sabine,
André Sabine,
Gabius HansJoachim,
Romero Antonio
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000023
Subject(s) - galectin , lectin , chimera (genetics) , c type lectin , glycan , galectin 3 , orthorhombic crystal system , chemistry , peptide , biology , crystallography , biochemistry , glycoprotein , crystal structure , gene , immunology
How lectins translate sugar‐encoded information into cellular effects not only depends on glycan recognition. Other domains of the protein can contribute to the functional profile of a lectin. Human galectin‐3 (Gal‐3), an adhesion/growth‐regulatory galectin, is composed of three different domains and is thus called a chimera‐type protein. In addition to the carbohydrate‐recognition domain, this lectin encompasses an N‐terminal domain consisting of a peptide harbouring two phosphorylation sites and nine non‐triple‐helical collagen‐like repeats. This region plays an as yet structurally undefined role in Gal‐3 aggregation and ligand recognition. To date, crystallization of full‐length Gal‐3 has not been achieved. With the aim of providing structural insights into this modular organization, a Gal‐3 variant was crystallized maintaining the terminal peptide and three of the nine collagen‐like repeats. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 94.04, b = 97.96, c = 236.20 Å, and diffracted to a resolution of 3.3 Å.