Summary for 4FQZ
Entry DOI | 10.2210/pdb4fqz/pdb |
Related | 3VKL 3VKM |
Related PRD ID | PRD_900004 |
Descriptor | Galectin-8, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | carbohydrate/sugar binding, sugar binding protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasmic vesicle : O00214 |
Total number of polymer chains | 1 |
Total formula weight | 34073.12 |
Authors | Yoshida, H.,Kamitori, S. (deposition date: 2012-06-26, release date: 2012-07-11, 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 Cited by 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: 22913484DOI: 10.1111/j.1742-4658.2012.08753.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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