rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
1998-11-19
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pubmed:databankReference |
|
pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
1072-8368
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
965-9
|
pubmed:dateRevised |
2009-12-11
|
pubmed:meshHeading |
pubmed-meshheading:9808041-Amino Acid Sequence,
pubmed-meshheading:9808041-Animals,
pubmed-meshheading:9808041-Aspartylglucosylaminase,
pubmed-meshheading:9808041-Carrier Proteins,
pubmed-meshheading:9808041-Crystallography, X-Ray,
pubmed-meshheading:9808041-Drosophila Proteins,
pubmed-meshheading:9808041-Dyneins,
pubmed-meshheading:9808041-Enzyme Inhibitors,
pubmed-meshheading:9808041-Models, Molecular,
pubmed-meshheading:9808041-Molecular Sequence Data,
pubmed-meshheading:9808041-Nitric Oxide Synthase,
pubmed-meshheading:9808041-Nitric Oxide Synthase Type I,
pubmed-meshheading:9808041-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9808041-Protein Structure, Secondary,
pubmed-meshheading:9808041-Rats
|
pubmed:year |
1998
|
pubmed:articleTitle |
Solution structure of a protein inhibitor of neuronal nitric oxide synthase.
|
pubmed:affiliation |
Department of Biochemistry, The Hong Kong University of Science and Technology, Kowloon, P.R. China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|