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J. Biol. Chem., Vol. 278, Issue 44, 43550-43555, October 31, 2003

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Hyaluronan Recognition Mode of CD44 Revealed by Cross-saturation and Chemical Shift Perturbation Experiments^*

Mitsuhiro Takeda, Hiroaki Terasawa, Masayoshi Sakakura, Yoshiki Yamaguchi, Masahiro Kajiwara¶, Hiroto Kawashima||, Masayuki Miyasaka||, and Ichio Shimada**

From the Graduate School of Pharmaceutical Sciences, the University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, the Japan Biological Information Research Center (JBIRC), Japan Biological Informatics Consortium (JBIC), Hatchobori, Chuo-ku, Tokyo 104-0032, Japan, the ^¶Department of Medicinal Chemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose-shi, Tokyo 204-8588, Japan, the ^||Laboratory of Molecular and Cellular Recognition, Osaka University Graduate School of Medicine, 2-2, Yamada-oka, Suita 565-0871, Japan, and the ^**Biological Information Research Center (BIRC), National Institute of Advanced Industrial Science and Technology (AIST), Aomi, Koto-ku, Tokyo 135-0064, Japan

CD44 is the main cell surface receptor for hyaluronic acid (HA) and contains a functional HA-binding domain (HABD) composed of a Link module with N- and C-terminal extensions. The contact residues of human CD44 HABD for HA have been determined by cross-saturation experiments and mapped on the topology of CD44 HABD, which we elucidated by NMR. The contact residues are distributed in both the consensus fold for the Link module superfamily and the additional structural elements consisting of the flanking regions. Interestingly, the contact residues exhibit small changes in chemical shift upon HA binding. In contrast, the residues with large chemical shift changes are localized in the C-terminal extension and the first -helix and are generally inconsistent with the contact residues. These results suggest that, upon ligand binding, the C-terminal extension and the first -helix undergo significant conformational changes, which may account for the broad ligand specificity of CD44 HABD.

Received for publication, July 28, 2003 , and in revised form, August 15, 2003.

^* This work was supported by a grant from the Japan New Energy and Industrial Technology Development Organization (NEDO) and Ministry of Economy, Trade and Industry (METI). 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.

To whom correspondence should be addressed: Graduate School of Pharmaceutical Sciences, the University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Tel./Fax: 81-3-3815-6540; E-mail: shimada{at}iw-nmr.f.u-tokyo.ac.jp.

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