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| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9334294 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9334294 | pubmed:issue | 5337 | lld:pubmed |
| pubmed-article:9334294 | pubmed:dateCreated | 1997-11-5 | lld:pubmed |
| pubmed-article:9334294 | pubmed:abstractText | The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOSox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged beta sheet engenders a curved alpha-beta domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis. | lld:pubmed |
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| pubmed-article:9334294 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9334294 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9334294 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9334294 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9334294 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:WuCC | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:GetzoffE DED | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:TainerJ AJA | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:GhoshD KDK | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:CraneB RBR | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:StuehrD JDJ | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:GachhuiRR | lld:pubmed |
| pubmed-article:9334294 | pubmed:author | pubmed-author:ArvaiA SAS | lld:pubmed |
| pubmed-article:9334294 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9334294 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9334294 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:9334294 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9334294 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9334294 | pubmed:pagination | 425-31 | lld:pubmed |
| pubmed-article:9334294 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9334294 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9334294 | pubmed:articleTitle | The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. | lld:pubmed |
| pubmed-article:9334294 | pubmed:affiliation | Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:9334294 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9334294 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9334294 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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