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J Biol Chem, Vol. 273, Issue 50, 33472-33481, December 11, 1998

Protein Inhibitor of Neuronal Nitric-oxide Synthase, PIN, Binds to a 17-Amino Acid Residue Fragment of the Enzyme

Jing-Song Fan, Qiang Zhang, Ming Li, Hidehito Tochio, Toshio Yamazaki^§, Masato Shimizu^¶, and Mingjie Zhang

From the  Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China, the ^§ Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan, and the ^¶ Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan

Neuronal nitric-oxide synthase (nNOS) is the primary nitric oxide (NO) regulator in neurons. The activity of the enzyme is inhibited by a protein inhibitor called PIN. We were able to purify large quantities of PIN overexpressed in bacterial cells. Analytical ultracentrifugation and chemical cross-linking studies showed that PIN exists as a monomer at low concentrations. The protein forms a high order aggregate at elevated concentrations. We have shown, using NMR spectroscopy, that the previously identified PIN-binding domain (PINB) of nNOS (residues 161-245) adopts a random coil structure in solution. By titrating ¹⁵N-labeled PINB with unlabeled PIN, the PIN-binding region of nNOS was precisely mapped to a 17-residue peptide fragment from Met-228 to His-244 of nNOS. NMR titration experiments also showed that PIN binds to nNOS with a 1:2 stoichiometry. A synthetic peptide corresponding to the identified PIN-binding region of nNOS was used to study the interaction between PIN and nNOS in detail. The functional implications of the results obtained from this study are discussed.

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