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J. Biol. Chem., Vol. 282, Issue 38, 28246-28255, September 21, 2007

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Structural Basis for Recognition of High Mannose Type Glycoproteins by Mammalian Transport Lectin VIP36^*

Tadashi Satoh, Nathan P. Cowieson¹, Wataru Hakamata^¶, Hiroko Ideo^||**, Keiko Fukushima^||**, Masaaki Kurihara^¶, Ryuichi Kato, Katsuko Yamashita^||**, and Soichi Wakatsuki²

From the Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia, ^¶Division of Organic Chemistry, National Institute of Health Sciences (NIHS), Tokyo 158-8501, Japan, ^||Innovative Research Initiatives, Tokyo Institute of Technology, Yokohama 226-8503, Japan, and ^**Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency, Tokyo 101-0062, Japan

VIP36 functions as a transport lectin for trafficking certain high mannose type glycoproteins in the secretory pathway. Here we report the crystal structure of VIP36 exoplasmic/luminal domain comprising a carbohydrate recognition domain and a stalk domain. The structures of VIP36 in complex with Ca²⁺ and mannosyl ligands are also described. The carbohydrate recognition domain is composed of a 17-stranded antiparallel -sandwich and binds one Ca²⁺ adjoining the carbohydrate-binding site. The structure reveals that a coordinated Ca²⁺ ion orients the side chains of Asp¹³¹, Asn¹⁶⁶, and His¹⁹⁰ for carbohydrate binding. This result explains the Ca²⁺-dependent carbohydrate binding of this protein. The Man--1,2-Man--1,2-Man, which corresponds to the D1 arm of high mannose type glycan, is recognized by eight residues through extensive hydrogen bonds. The complex structures reveal the structural basis for high mannose type glycoprotein recognition by VIP36 in a Ca²⁺-dependent and D1 arm-specific manner.

Received for publication, April 11, 2007 , and in revised form, June 25, 2007.

The atomic coordinates and structure factors (code 2DUO, 2DUP, 2DUQ, 2DUR, and 2E6V) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by the Protein 3000 project, by Grant-in-aid for Young Scientists (B) 17790097 from The Ministry of Education, Culture, Sports, Science and Technology of Japan, and by research grants for research on human immunodeficiency virus/AIDS from The Ministry of Health and Labor Sciences of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1-4.

¹ Supported by a fellowship from the Australian Synchrotron Research Program.

² To whom correspondence should be addressed. Tel.: 81-29-864-5631; Fax: 81-29-879-6179; E-mail: soichi.wakatsuki{at}kek.jp.

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