6FOF

Crystal structure of a crystallized variant of h-Gal3: Gal-3[NTS/VII-IX]

Summary for 6FOF

• Entry DOI: 10.2210/pdb6fof/pdb
• Related PRD ID: PRD_900004
• Descriptor: Galectin-3,Galectin-3, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: galectin, apoptosis, glycosylation, sugar binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 260931.25

Authors

Romero, A.,Flores-Ibarra, A.,Medrano, F.J. (deposition date: 2018-02-07, release date: 2018-07-18, Last modification date: 2024-01-17)

Primary citation

Flores-Ibarra, A.,Vertesy, S.,Medrano, F.J.,Gabius, H.J.,Romero, A.
Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.
Sci Rep, 8:9835-9835, 2018

PubMed 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.

PubMed: 29959397
DOI: 10.1038/s41598-018-28235-x

Experimental method

X-RAY DIFFRACTION (2.2 Å)