6l6d

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X-ray structure of human galectin-10 in complex with D-N-acetylgalactosamine

Structural highlights

6l6d 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 1.93Å
Ligands:NGA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG10_HUMAN Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg).[1]

Publication Abstract from PubMed

The galectins are a family of beta-galactoside-specific animal lectins, and have attracted much attention as novel regulators of the immune system. Galectin-10 is well-expressed in eosinophils, and spontaneously forms Charcot-Leyden crystals (CLCs), during prolonged eosinophilic inflammatory reactions, which are frequently observed in eosinophilic diseases. Although biochemical and structural characterizations of galectin-10 have been done, its biological role and molecular mechanism are still unclear, and few X-ray structures of galectin-10 in complex with monosaccharides/oligosaccharides have been reported. Here, X-ray structures of galectin-10 in complexes with seven monosaccharides are presented with biochemical analyses to detect interactions of galectin-10 with monosaccharides/oligosaccharides. Galectin-10 forms a homo-dimer in the face-to-face orientation, and the monosaccharides bind to the carbohydrate recognition site composed of amino acid residues from two galectin-10 molecules of dimers, suggesting that galectin-10 dimer likely captures the monosaccharides in solution and in vivo. d-Glucose, d-allose, d-arabinose, and D-N-acetylgalactosamine bind to the interfaces between galectin-10 dimers in crystals, and they affect the stability of molecular packing in crystals, leading to easy-dissolving of CLCs, and/or inhibiting the formation of CLCs. These monosaccharides may serve as effectors of G10 to form CLCs in vivo.

Structures of human galectin-10/monosaccharide complexes demonstrate potential of monosaccharides as effectors in forming Charcot-Leyden crystals.,Itoh A, Nonaka Y, Nakakita SI, Yoshida H, Nishi N, Nakamura T, Kamitori S Biochem Biophys Res Commun. 2020 Feb 17. pii: S0006-291X(20)30303-X. doi:, 10.1016/j.bbrc.2020.02.037. PMID:32081418[2]

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

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See Also

References

  1. Kubach J, Lutter P, Bopp T, Stoll S, Becker C, Huter E, Richter C, Weingarten P, Warger T, Knop J, Mullner S, Wijdenes J, Schild H, Schmitt E, Jonuleit H. Human CD4+CD25+ regulatory T cells: proteome analysis identifies galectin-10 as a novel marker essential for their anergy and suppressive function. Blood. 2007 Sep 1;110(5):1550-8. doi: 10.1182/blood-2007-01-069229. Epub 2007 May, 14. PMID:17502455 doi:http://dx.doi.org/10.1182/blood-2007-01-069229
  2. Itoh A, Nonaka Y, Nakakita SI, Yoshida H, Nishi N, Nakamura T, Kamitori S. Structures of human galectin-10/monosaccharide complexes demonstrate potential of monosaccharides as effectors in forming Charcot-Leyden crystals. Biochem Biophys Res Commun. 2020 Feb 17. pii: S0006-291X(20)30303-X. doi:, 10.1016/j.bbrc.2020.02.037. PMID:32081418 doi:http://dx.doi.org/10.1016/j.bbrc.2020.02.037

Contents


PDB ID 6l6d

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