3VKN

Galectin-8 N-terminal domain in free form

Summary for 3VKN

• Entry DOI: 10.2210/pdb3vkn/pdb
• Related: 3VKL 3VKM 3VKO
• Descriptor: Galectin-8, CHLORIDE ION (3 entities in total)
• Functional Keywords: bete-sandwich, carbohydrate binding, oligosaccharide, sugar binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (Probable): O00214
• Total number of polymer chains: 2
• Total formula weight: 34771.67

Authors

Kamitori, S.,Yoshida, H. (deposition date: 2011-11-18, release date: 2012-09-12, Last modification date: 2023-11-08)

Primary citation

Yoshida, H.,Yamashita, S.,Teraoka, M.,Itoh, A.,Nakakita, S.,Nishi, N.,Kamitori, S.
X-ray structure of a protease-resistant mutant form of human galectin-8 with two carbohydrate recognition domains
Febs J., 279:3937-3951, 2012

PubMed Abstract: Galectin-8 is a tandem-repeat-type β-galactoside-specific animal lectin possessing N-terminal and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively), with a difference in carbohydrate-binding specificity, involved in cell-matrix interaction, malignant transformation, and cell adhesion. N-CRD shows strong affinity for α2-3-sialylated oligosaccharides, a feature unique to galectin-8. C-CRD usually shows lower affinity for oligosaccharides but higher affinity for N-glycan-type branched oligosaccharides than does N-CRD. There have been many structural studies on galectins with a single carbohydrate recognition domain (CRD), but no X-ray structure of a galectin containing both CRDs has been reported. Here, the X-ray structure of a protease-resistant mutant form of human galectin-8 possessing both CRDs and the novel pseudodimer structure of galectin-8 N-CRD in complexes with α2-3-sialylated oligosaccharide ligands were determined. The results revealed a difference in specificity between N-CRD and C-CRD, and provided new insights into the association of CRDs and/or molecules of galectin-8.

PubMed: 22913484
DOI: 10.1111/j.1742-4658.2012.08753.x

Experimental method

X-RAY DIFFRACTION (1.98 Å)