4hl0

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hl0 OCA], [https://pdbe.org/4hl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hl0 RCSB], [https://www.ebi.ac.uk/pdbsum/4hl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hl0 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The full-length crystal structure of Toxascaris leonine galectin (Tl-gal), a galectin-9 homologue protein, was determined at a resolution of 2.0 A. Galectin-9 exhibits a variety of biological functions, including cell aggregation, eosinophil chemoattraction, activation and apoptosis of murine thymocytes, T cells and human melanoma cells. Similar to this galectin, Tl-gal may function as a regulatory molecule in the host immune system; however, no molecular or structural information has been reported for Tl-gal. Moreover, until now, there have been no reports of a full-length galectin structure. There are two molecules of Tl-gal per asymmetric unit in space group P2(1)2(1)2(1), and the N-terminal and C-terminal carbohydrate-recognition domains (NCRD and CCRD) of Tl-gal are composed of six-stranded beta-sheets and five-stranded beta-sheets with a short alpha-helix. The NCRD of Tl-gal resembles that of human galectin-7 and its CCRD resembles human galectin-9, but the residues in the interface and loop regions of the NCRD and CCRD are flexible and are related to interaction. Engagement of the T-cell immunoglobulin mucin-3 (Tim-3) immunoglobulin variable (IgV) domain by a galectin-9 ligand is known to be important for appropriate termination of T-helper 1 immune responses. To investigate the binding site of Tl-gal, the interaction between Tl-gal and Tim-3 was modelled. Tim-3 is docked into a major groove of the Tl-gal structure, which is larger and deeper than the minor groove. The structural information presented here will provide insight into the development of novel anti-inflammatory agents or selective modulators of immune response.

Structure of full-length Toxascaris leonina galectin with two carbohydrate-recognition domains.,Jeong MS, Hwang HG, Yu HS, Jang SB Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):168-75. doi:, 10.1107/S0907444912045106. Epub 2013 Jan 16. PMID:23385453<ref>PMID:23385453</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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