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J. Biol. Chem., Vol. 280, Issue 37, 32372-32378, September 16, 2005

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Structural Characterization of Calcineurin B Homologous Protein 1^*

Youichi Naoe, Kyouhei Arita, Hiroshi Hashimoto, Hiroshi Kanazawa, Mamoru Sato, and Toshiyuki Shimizu1

From the International Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan, and Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama-cho 1-16, Toyonaka, Osaka 560-0043, Japan

Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding EF-hand protein that plays a role in membrane trafficking. It binds to multiple effector proteins, including Na⁺/H⁺ exchangers, a serine/threonine kinase, and calcineurin, potentially modulating their function. The crystal structure of calcium-bound CHP1 from rat has been determined at 2.2 Å of resolution. The molecule has a compact -helical structure containing four EF-hands. The overall folding topology of the protein is similar to that of the regulatory B subunit of calcineurin and to that of calcium- and integrin-binding protein. The calcium ion is coordinated in typical fashion in the third and fourth EF-hands, but the first and second EF-hands contain no calcium ion. The first EF-hand is maintained by internal interactions, and the second EF-hand is stabilized by hydrophobic interactions. CHP1 contains a hydrophobic pocket on the opposite side of the protein to the EF-hands that has been implicated in ligand binding.

Received for publication, March 28, 2005 , and in revised form, June 23, 2005.

The atomic coordinates and structure factors (code 2CT9) 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 by Grant-in-aid (14780515) for Young Scientists (B) from the Japan Society of the Promotion of Science (JSPS) (to H. H.), Grant-in-aid (15570101) for Scientific Research (C) from the JSPS (to T. S.), Grants-in-aid for Scientific Research on Priority Areas (13142207) (to H. K.) and (16048226) (to H. H.), and by the Protein 3000 Project of The Ministry of Education, Culture, Sports, Science, and Technology. 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.

¹ To whom correspondence should be addressed: International Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan. Tel.: 81-45-508-7226; Fax: 81-45-508-7365; E-mail: shimizu{at}tsurumi.yokohama-cu.ac.jp.

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