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Crystal structure of a crystallized variant of h-Gal3: Gal-3[NTS/VII-IX]Crystal structure of a crystallized variant of h-Gal3: Gal-3[NTS/VII-IX]
Structural highlights
Function[LEG3_HUMAN] Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells.[1] [2] [3] Publication Abstract from PubMedAmong 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 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. Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.,Flores-Ibarra A, Vertesy S, Medrano FJ, Gabius HJ, Romero A Sci Rep. 2018 Jun 29;8(1):9835. doi: 10.1038/s41598-018-28235-x. PMID:29959397[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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