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Protein Science (2007), 16:329-335. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Crystal structure of human µ-crystallin complexed with NADPH

Zhongjun Cheng1,2,4, Lihua Sun3,4, Jianhua He3, and Weimin Gong1,2

1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China
2 School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China
3 Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, People's Republic of China

(RECEIVED September 12, 2006; FINAL REVISION November 15, 2006; ACCEPTED November 15, 2006)

Human cytosolic 3,5,3'-triiodo-L-thyronine-binding protein, also called µ-crystallin or CRYM, plays important physiological roles in transporting 3,5,3'-triiodo-L-thyronine (T3) into nuclei and regulating thyroid-hormone-related gene expression. The crystal structure of human CRYM's bacterial homolog Pseudomonas putida ornithine cyclodeaminase and Archaeoglobus fulgidus alanine dehydrogenase have been available, but no CRYM structure has been reported. Here, we report the crystal structure of human CRYM bound with NADPH refined to 2.6 Å, and there is one dimer in the asymmetric unit. The structure contains two domains: a Rossmann fold–like NADPH-binding domain and a dimerization domain. Different conformations of the loop Arg83–His92 have been observed in two monomers of human CRYM in the same asymmetric unit. The peptide bond of Val89–Pro90 is a trans-configuration in one monomer but a cis-configuration in the other. A detailed comparison of the human µ-crystallin structure with its structurally characterized homologs including the overall comparison and superposition of active sites was conducted. Finally, a putative T3-binding site in human CRYM is proposed based on comparison with structural homologs.

Keywords: µ-crystallin; p38 cytosolic 3,5,3'-triiodo-L-thyronine-binding protein; crystal structure; cis/trans isomerization of proline; T3-binding site; nonsyndromic deafness


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