Masamichi Nagae, Nozomu Nishi, Takeomi Murata, Taichi Usui, Takanori Nakamura, Soichi Wakatsuki, Ryuichi Kato
Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, Japan.
Glycobiology 2009 FebGalectins 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.
Masamichi Nagae, Nozomu Nishi, Takeomi Murata, Taichi Usui, Takanori Nakamura, Soichi Wakatsuki, Ryuichi Kato. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology. 2009 Feb;19(2):112-7
PMID: 18977853
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