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3VKL

Protease-resistant mutant form of human Galectin-8 in complex with two lactose molecules

Summary for 3VKL
Entry DOI10.2210/pdb3vkl/pdb
Related3VKM 3VKN 3VKO 4FQZ
Related PRD IDPRD_900004
DescriptorGalectin-8, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsbeta-sandwich, carbohydrate binding, oligosaccharide, sugar binding protein
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasmic vesicle : O00214
Total number of polymer chains2
Total formula weight68830.83
Authors
Kamitori, S.,Yoshida, H. (deposition date: 2011-11-18, release date: 2012-09-12, Last modification date: 2023-11-08)
Primary citationYoshida, 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: 22913484
DOI: 10.1111/j.1742-4658.2012.08753.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

226707

數據於2024-10-30公開中

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