1qw4

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(New page: 200px<br /><applet load="1qw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qw4, resolution 2.4&Aring;" /> '''Crystal Structure of ...)
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[[Image:1qw4.jpg|left|200px]]<br /><applet load="1qw4" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1qw4, resolution 2.4&Aring;" />
'''Crystal Structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in complex with N-omega-propyl-L-arginine.'''<br />
'''Crystal Structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in complex with N-omega-propyl-L-arginine.'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1QW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN, HEM, H4B and 3AR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QW4 OCA].
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1QW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=H4B:'>H4B</scene> and <scene name='pdbligand=3AR:'>3AR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW4 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fedorov, R.]]
[[Category: Fedorov, R.]]
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[[Category: Ghosh, D.K.]]
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[[Category: Ghosh, D K.]]
[[Category: Hartmann, E.]]
[[Category: Hartmann, E.]]
[[Category: Schlichting, I.]]
[[Category: Schlichting, I.]]
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[[Category: inosoxy inhibitor complex]]
[[Category: inosoxy inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:03:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:20 2008''

Revision as of 12:44, 21 February 2008


1qw4, resolution 2.4Å

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Crystal Structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in complex with N-omega-propyl-L-arginine.

Overview

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.

About this Structure

1QW4 is a Single protein structure of sequence from Mus musculus with , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

Reference

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 DK, Schlichting I, J Biol Chem. 2003 Nov 14;278(46):45818-25. Epub 2003 Sep 3. PMID:12954642

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