6ljp

From Proteopedia

Crystal structure of human galectin-16

Structural highlights

6ljp is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG16_HUMAN Binds lactose with high affinity. Strong inducer of T-cell apoptosis.^[1]

Publication Abstract from PubMed

BACKGROUND: The structure of human galectin-16 (Gal-16) has yet to be solved, and its function has remained elusive. METHODS: X-ray crystallography was used to determine the atomic structures of Gal-16 and two of its mutants. The Gal-16 oligomer state was investigated by gel filtration, its hemagglutination activity was determined along with its ability to bind lactose using ITC. The cellular distribution of EGFP-tagged Gal-16 in various cell lines was also investigated, and the interaction between Gal-16 and c-Rel was assessed by pull-down studies, microscale thermophoresis and immunofluorescence. RESULTS: Unlike other galectins, Gal-16 lacks the ability to bind the beta-galactoside lactose. Lactose binding could be regained by replacing an arginine (Arg55) with asparagine, as shown in the crystal structures of two lactose-loaded Gal-16 mutants (R55N and R55N/H57R). Gal-16 was also shown to be monomeric by gel filtration, as well as in crystal structures. Thus, this galectin could not induce erythrocyte agglutination. EGFP-tagged Gal-16 was found to be localized mostly in the nucleus of various cell types, and can interact with c-Rel, a member of NF-kappaB family. CONCLUSIONS: Gal-16 exists as a monomer and its ligand binding is significantly different from that of other prototype galectins, suggesting that it has a novel function(s). The interaction between Gal-16 and c-Rel indicates that Gal-16 may regulate signal transduction pathways via the c-Rel hub in B or T cells at the maternal-fetal interface. GENERAL SIGNIFICANCE: The present study lays the foundation for further studies into the cellular and physiological functions of Gal-16.

Human galectin-16 has a pseudo ligand binding site and plays a role in regulating c-Rel-mediated lymphocyte activity.,Si Y, Yao Y, Jaramillo Ayala G, Li X, Han Q, Zhang W, Xu X, Tai G, Mayo KH, Zhou Y, Su J Biochim Biophys Acta Gen Subj. 2020 Oct 2;1865(1):129755. doi:, 10.1016/j.bbagen.2020.129755. PMID:33011338^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Than NG, Romero R, Goodman M, Weckle A, Xing J, Dong Z, Xu Y, Tarquini F, Szilagyi A, Gal P, Hou Z, Tarca AL, Kim CJ, Kim JS, Haidarian S, Uddin M, Bohn H, Benirschke K, Santolaya-Forgas J, Grossman LI, Erez O, Hassan SS, Zavodszky P, Papp Z, Wildman DE. A primate subfamily of galectins expressed at the maternal-fetal interface that promote immune cell death. Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9731-6. doi:, 10.1073/pnas.0903568106. Epub 2009 Jun 2. PMID:19497882 doi:http://dx.doi.org/10.1073/pnas.0903568106
↑ Si Y, Yao Y, Jaramillo Ayala G, Li X, Han Q, Zhang W, Xu X, Tai G, Mayo KH, Zhou Y, Su J. Human galectin-16 has a pseudo ligand binding site and plays a role in regulating c-Rel-mediated lymphocyte activity. Biochim Biophys Acta Gen Subj. 2020 Oct 2;1865(1):129755. doi:, 10.1016/j.bbagen.2020.129755. PMID:33011338 doi:http://dx.doi.org/10.1016/j.bbagen.2020.129755