1qw6
From Proteopedia
(New page: 200px<br /><applet load="1qw6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qw6, resolution 2.1Å" /> '''Rat neuronal nitric o...) |
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| - | [[Image:1qw6.jpg|left|200px]]<br /><applet load="1qw6" size=" | + | [[Image:1qw6.jpg|left|200px]]<br /><applet load="1qw6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qw6, resolution 2.1Å" /> | caption="1qw6, resolution 2.1Å" /> | ||
'''Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.'''<br /> | '''Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The high level of amino acid conservation and structural similarity in the | + | 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== | ||
| - | 1QW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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:// | + | 1QW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1QW6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fedorov, R.]] | [[Category: Fedorov, R.]] | ||
| - | [[Category: Ghosh, D | + | [[Category: Ghosh, D K.]] |
[[Category: Hartmann, E.]] | [[Category: Hartmann, E.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
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[[Category: rat nnosoxy complex with n-omega-propyl-l-arg]] | [[Category: rat nnosoxy complex with n-omega-propyl-l-arg]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:21 2008'' |
Revision as of 12:44, 21 February 2008
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Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.
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
1QW6 is a Single protein structure of sequence from Rattus norvegicus 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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