2ZHK

Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine dimer (crystal 1)

Summary for 2ZHK

• Entry DOI: 10.2210/pdb2zhk/pdb
• Related: 2ZHL 2ZHM 2ZHN
• Descriptor: Galectin-9, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: beta sandwich, carbohydrate binding protein, galectin, secreted, sugar binding protein
• Biological source: HOMO SAPIENS (human)
• Cellular location: Cytoplasm (By similarity): O00182
• Total number of polymer chains: 2
• Total formula weight: 34214.07

Authors

Nagae, M.,Nishi, N.,Murata, T.,Usui, T.,Nakamura, T.,Wakatsuki, S.,Kato, R. (deposition date: 2008-02-06, release date: 2008-12-30, Last modification date: 2024-03-13)

Primary citation

Nagae, M.,Nishi, N.,Murata, T.,Usui, T.,Nakamura, T.,Wakatsuki, S.,Kato, R.
Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain.
Glycobiology, 19:112-117, 2009

PubMed Abstract: Galectins are a family of beta-galactoside-specific lectins bearing a conserved carbohydrate recognition domain. Interactions between galectins and poly-N-acetyllactosamine sequences are critical in a variety of biological processes. Galectin-9, a member of the galectin family, has two carbohydrate recognition domains at both the N- and C-terminal regions. Here we report the crystal structure of the human galectin-9 N-terminal carbohydrate recognition domain in complex with N-acetyllactosamine dimers and trimers. These complex structures revealed that the galectin-9 N-terminal carbohydrate recognition domain can recognize internal N-acetyllactosamine units within poly-N-acetyllactosamine chains. Based on these complex structures, we propose two putative recognition modes for poly-N-acetyllactosamine binding by galectins.

PubMed: 18977853
DOI: 10.1093/glycob/cwn121

Experimental method

X-RAY DIFFRACTION (1.8 Å)