Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.
Andrea Flores-IbarraSabine VértesyFrancisco J MedranoHans-Joachim GabiusAntonio RomeroPublished in: Scientific reports (2018)
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.
Keyphrases
- endothelial cells
- low density lipoprotein
- electronic health record
- transcription factor
- genome wide
- big data
- staphylococcus aureus
- induced pluripotent stem cells
- biofilm formation
- computed tomography
- magnetic resonance imaging
- escherichia coli
- machine learning
- amino acid
- gene expression
- protein protein
- single cell
- small molecule
- deep learning
- binding protein