<scp>X</scp>‐ray structure of a protease‐resistant mutant form of human galectin‐8 with two carbohydrate recognition domains

Yoshida, Hiromi; Yamashita, Satoshi; Teraoka, Misa; Itoh, Akichika; Nakakita, Shin Ichi; Nishi, Nozomu; Kamitori, Shigehiro

doi:10.1111/j.1742-4658.2012.08753.x

Cited by 39 publications

(45 citation statements)

References 47 publications

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“…S4) because it has been reported that GAL8 forms a dimer in vitro through its N-CRD 23 . Furthermore, the proposed dimer models of GAL8 are all different from our observations 19,20 . Therefore, we assessed the oligomeric state of GAL8 in solution, which showed clear monomer formation (Supplementary Fig.…”

Section: Resultscontrasting

confidence: 99%

“…SEC-MALS data of GAL8 and N-CRD of GAL8 in the presence of NAD showed the same result as those in the absence of NAD (Supplementary Figs S1b and S9), suggesting that NAD has no effect on dimerization and also that GAL8 exists as a monomer in solution. The indole ring of Trp86 forms van der Waals contacts with one of the pentose rings of NAD in a similar manner observed in other galectins 13,19,20 , and the tryptophan residue is strictly conserved among all galectins (Supplementary Fig. S6).…”

Section: Resultssupporting

confidence: 59%

“…4a; Supplementary Fig. S6) 19,20,24 . However, our complex structure showed that NDP52 only binds to the C-CRD.…”

Section: Resultsmentioning

confidence: 99%

“…Finally, proteins were loaded onto a 16/60 Superdex75 gel filtration column (GE Healthcare) pre-equilibrated with 50 mM HEPES (pH 7.0), 200 mM NaCl and 1 mM TCEP. The structural study was not straightforward, and therefore we shortened the long linker between N-CRD (residues Met1-Ser155) and C-CRD (residues Arg184-Trp317) based on previous reports 20,22 . This linker-shortened version of GAL8 was overexpressed and purified in a similar manner as the full-length protein.…”

Section: Methodsmentioning

confidence: 99%

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Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

et al. 2013

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Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N-and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.

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Section: Resultscontrasting

confidence: 99%

Section: Resultssupporting

confidence: 59%

“…4a; Supplementary Fig. S6) 19,20,24 . However, our complex structure showed that NDP52 only binds to the C-CRD.…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

et al. 2013

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“…Tandem-repeat type galectins are sensitive to proteases due to the long linker. To carry out X-ray crystal structure determinations of tandem-repeat type galectins with two CRDs, the galectins with a short linker (19) and/ or the protease-resistant mutant forms with a modified linker peptide were used (20)(21)(22).…”

Section: A Introductionmentioning

confidence: 99%

Three-Dimensional Structures of Galectins

Kamitori

2018

TIGG

Self Cite

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The galectins are a family of β-galactoside-specific animal lectins that contain a conserved carbohydrate recognition domain (CRD) with approximately 140 amino acid residues. There are 14 members in the mammalian galectin family (galectin-1-10, and 11-15), and they have different specificities for oligosaccharides. X-ray structures of the galectin CRD in complexes with oligosaccharides have provided important clues about the oligosaccharide-recognition mechanisms of galectins giving the different specificities. Galectin is divalent in glycan binding due to the association of two CRDs that crosslink with oligosaccharides. The spatial arrangement of the two CRDs is very important for elucidating the biological functions of galectins. Several different spatial arrangements of CRDs are found in X-ray structures of galectins. I herein examined the three-dimensional structures of galectins relevant for biological functions, based on the protein-ligand interactions related with oligosaccharide-specificity, the cross-linking structure by galectin and oligosaccharides, and the spatial arrangements of CRDs. A. IntroductionThe galectins are a family of β-galactoside-specific animal lectins that contain a conserved carbohydrate recognition domain In this review, I examined three-dimensional structures of galectins based on the protein-ligand interactions related with oligosaccharide-specificity, the cross-linking structure by galectin and oligosaccharides, and the spatial arrangements of CRDs of the prototype and tandem-repeat type galectins. 2,7,8,9, 10 stand for human galectin-1, 2, 7, 8, 9, 10, respectively (unless stated otherwise). Figures 2, 3, 4, 5 were drawn with the program PyMOL(23). B. Three-Dimensional Structure of Galectin CRDThe overall structure of galectin-9_C-CRD in complex with LacNAc (galectin-9_C-CRD/LacNAc (PDB ID: 3NV2)) (17) is MINIREVIEW

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Combining Crystallography and Hydrogen–Deuterium Exchange to Study Galectin–Ligand Complexes

Ruiz

Ulrich

Lindner

et al. 2015

Chemistry A European J

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The physiological significance arising from translating information stored in glycans into cellular effects explains the interest in structurally defining lectin-carbohydrate recognition. The relatively small set of adhesion/growth-regulatory galectins in chicken makes this system attractive to study the origins of specificity and divergence. Cell binding by using glycosylation mutants reveals binding of the N-terminal domain of chicken galectin-8 (CG-8N) to α-2,3-sialylated and galactose-terminated glycan chains. Cocrystals with lactose and its 3'-sialylated derivative disclose Arg58 as a key contact for the carboxylic acid and differences in loop lengths to the three homodimeric chicken galectins. Monitoring hydrogen-deuterium exchange by mass spectrometry revealed an effective reduction of deuteration after ligand binding within the contact area. In addition, evidence for changes in solvent accessibility of amide protons beyond this site was obtained. Their detection, which highlights the sensor capacity of this technique, encourages systematic studies on galectins and beyond.

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X‐ray structure of a protease‐resistant mutant form of human galectin‐8 with two carbohydrate recognition domains

Cited by 39 publications

References 47 publications

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

Three-Dimensional Structures of Galectins

Combining Crystallography and Hydrogen–Deuterium Exchange to Study Galectin–Ligand Complexes

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