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  Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms

Fedorov, R., Hartmann, E., Ghosh, D. K., & Schlichting, I. (2003). Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms. The Journal of Biological Chemistry, 278(46), 45818-45825. doi:10.1074/jbc.M306030200.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0029-B1F0-1 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0029-B1F1-0
Genre: Journal Article
Alternative Title : Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms

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JBiolChem_278_2003_45818.pdf (Any fulltext), 797KB
 
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 Creators:
Fedorov, Roman1, Author           
Hartmann, Elisabeth1, Author           
Ghosh, Dipak K., Author
Schlichting, Ilme1, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The high level of amino acid conservation and structural similarity in the immediate vicinity of the substrate binding sites of the oxygenase domains of the nitric-oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, and nNOSoxy) make the interpretation of the structural basis of inhibitor isoform specificity a challenge and provide few clues for the design of new selective compounds. Crystal structures of iNOSoxy and nNOSoxy complexed with the inhibitors W1400 and Nomega-propyl-l-arginine provide a rationale for their isoform specificity. It involves differences outside the immediate active site as well as a conformational flexibility in the active site that allows the adoption of distinct conformations in response to interactions with the inhibitors. This flexibility is determined by isoform-specific residues outside the active site.

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Language(s): eng - English
 Dates: 2003-09-032003-06-092003-09-032003-09-032003-11-14
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665835
DOI: 10.1074/jbc.M306030200
URI: http://www.ncbi.nlm.nih.gov/pubmed/12954642
URI: http://www.jbc.org/cgi/content/full/278/46/45818
Other: 6048
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 278 (46) Sequence Number: - Start / End Page: 45818 - 45825 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1