Solution structure of a protein inhibitor of neuronal nitric oxide synthase.
The structure of the neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), has been determined by NMR spectroscopy. Two N-terminal antiparallel alpha-helices pack against a four-stranded antiparallel beta-sheet in the C-terminal region of the protein, forming a two-layer alpha/beta plait. The three dimensional structure of PIN resembles the fold of the B-chain of aspartylglucosaminidase. A non-prolyl cis peptide bond was found between Pro 52 and Thr 53 of the protein. PIN has a large solvent-exposed hydrophobic surface that contains a cavity and is rimmed with positive charges. This surface may serve as the primary target-binding region for this multi-functional regulatory protein.
Tochio
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Department of Biochemistry, The Hong Kong University of Science and Technology, Kowloon, P.R. China.
Ohki
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Zhang
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Li
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Zhang
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D000595:Amino Acid Sequence; D000818:Animals; D001227:Aspartylglucosylaminase / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins; D004398:Dyneins; D004791:Enzyme Inhibitors / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019001:Nitric Oxide Synthase / Q000037:antagonists & inhibitors*; D052248:Nitric Oxide Synthase Type I; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D051381:Rats
D002352:Carrier Proteins; D029721:Drosophila Proteins; D004791:Enzyme Inhibitors; D019001:Nitric Oxide Synthase; D052248:Nitric Oxide Synthase Type I; C496322:Nos1 protein, rat; D001227:Aspartylglucosylaminase; D004398:Dyneins