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Glycobiology Advance Access published online on October 31, 2008
Glycobiology, doi:10.1093/glycob/cwn121
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Communications

Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain

Masamichi Nagae1,#, Nozomu Nishi2, Takeomi Murata3, Taichi Usui3, Takanori Nakamura2, Soichi Wakatsuki1 and Ryuichi Kato1,*

1 Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan
2 Department of Endocrinlogy, Faculty of Medicine, Kagawa University, Kagawa 761-0793, Japan
3 Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan

* To whom correspondence should be addressed. Tel.: 81-29-879-6177; Fax: 81-29-879-6179; E-mail: ryuichi.kato{at}kek.jp

Received on April 24, 2008; accepted on October 27, 2008

Galectins are a family of β-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.

Key words: carbohydrate recognition / X-ray structure / galectin / poly-N-acetyllactosamine

# Present address: Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan


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