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rdf:type |
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lifeskim:mentions |
umls-concept:C0001128,
umls-concept:C0014442,
umls-concept:C0033684,
umls-concept:C0132555,
umls-concept:C0175718,
umls-concept:C0332255,
umls-concept:C0521390,
umls-concept:C1145667,
umls-concept:C1709915,
umls-concept:C1825012,
umls-concept:C1999216
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pubmed:issue |
50
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pubmed:dateCreated |
1999-1-14
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33472-81
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pubmed:dateRevised |
2009-12-11
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pubmed:meshHeading |
pubmed-meshheading:9837926-Amino Acid Sequence,
pubmed-meshheading:9837926-Animals,
pubmed-meshheading:9837926-Base Sequence,
pubmed-meshheading:9837926-Carrier Proteins,
pubmed-meshheading:9837926-DNA Primers,
pubmed-meshheading:9837926-Drosophila Proteins,
pubmed-meshheading:9837926-Dyneins,
pubmed-meshheading:9837926-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9837926-Molecular Sequence Data,
pubmed-meshheading:9837926-Nitric Oxide Synthase,
pubmed-meshheading:9837926-Nitric Oxide Synthase Type I,
pubmed-meshheading:9837926-Peptide Fragments,
pubmed-meshheading:9837926-Protein Binding,
pubmed-meshheading:9837926-Rats,
pubmed-meshheading:9837926-Recombinant Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme.
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pubmed:affiliation |
Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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