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1nsi
From Proteopedia
(New page: 200px<br /> <applet load="1nsi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsi, resolution 2.55Å" /> '''HUMAN INDUCIBLE NIT...) |
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| - | [[Image:1nsi.gif|left|200px]]<br /> | + | [[Image:1nsi.gif|left|200px]]<br /><applet load="1nsi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nsi" size=" | + | |
caption="1nsi, resolution 2.55Å" /> | caption="1nsi, resolution 2.55Å" /> | ||
'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX'''<br /> | '''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of the heme domain of human inducible nitric-oxide | + | The crystal structures of the heme domain of human inducible nitric-oxide synthase (NOS-2) in zinc-free and -bound states have been solved. In the zinc-free structure, two symmetry-related cysteine residues form a disulfide bond. In the zinc-bound state, these same two cysteine residues form part of a zinc-tetrathiolate (ZnS(4)) center indistinguishable from that observed in the endothelial isoform (NOS-3). As in NOS-3, ZnS(4) plays a key role in stabilizing intersubunit contacts and in maintaining the integrity of the cofactor (tetrahydrobiopterin) binding site of NOS-2. A comparison of NOS-2 and NOS-3 structures illustrates the conservation of quaternary structure, tertiary topology, and substrate and cofactor binding sites, in addition to providing insights on isoform-specific inhibitor design. The structural comparison also reveals that pterin binding does not preferentially stabilize the dimer interface of NOS-2 over NOS-3. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NSI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4, ZN, HEM, H4B, ARG and GOL 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:// | + | 1NSI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=H4B:'>H4B</scene>, <scene name='pdbligand=ARG:'>ARG</scene> and <scene name='pdbligand=GOL:'>GOL</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=1NSI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blasko, E.]] | [[Category: Blasko, E.]] | ||
| - | [[Category: Glaser, C | + | [[Category: Glaser, C B.]] |
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
| - | [[Category: Parkinson, J | + | [[Category: Parkinson, J F.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
| - | [[Category: Raman, C | + | [[Category: Raman, C S.]] |
[[Category: Whitlow, M.]] | [[Category: Whitlow, M.]] | ||
| - | [[Category: Young, T | + | [[Category: Young, T A.]] |
[[Category: ARG]] | [[Category: ARG]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: tetrahydrobiopterin]] | [[Category: tetrahydrobiopterin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:31 2008'' |
Revision as of 12:09, 21 February 2008
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HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX
Contents |
Overview
The crystal structures of the heme domain of human inducible nitric-oxide synthase (NOS-2) in zinc-free and -bound states have been solved. In the zinc-free structure, two symmetry-related cysteine residues form a disulfide bond. In the zinc-bound state, these same two cysteine residues form part of a zinc-tetrathiolate (ZnS(4)) center indistinguishable from that observed in the endothelial isoform (NOS-3). As in NOS-3, ZnS(4) plays a key role in stabilizing intersubunit contacts and in maintaining the integrity of the cofactor (tetrahydrobiopterin) binding site of NOS-2. A comparison of NOS-2 and NOS-3 structures illustrates the conservation of quaternary structure, tertiary topology, and substrate and cofactor binding sites, in addition to providing insights on isoform-specific inhibitor design. The structural comparison also reveals that pterin binding does not preferentially stabilize the dimer interface of NOS-2 over NOS-3.
Disease
Known diseases associated with this structure: Hypertension, susceptibility to OMIM:[163730], Malaria, resistance to OMIM:[163730]
About this Structure
1NSI is a Single protein structure of sequence from Homo sapiens with , , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase., Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL, J Biol Chem. 1999 Jul 23;274(30):21276-84. PMID:10409685
Page seeded by OCA on Thu Feb 21 14:09:31 2008
Categories: Homo sapiens | Nitric-oxide synthase | Single protein | Blasko, E. | Glaser, C B. | Li, H. | Parkinson, J F. | Poulos, T L. | Raman, C S. | Whitlow, M. | Young, T A. | ARG | GOL | H4B | HEM | SO4 | ZN | Heme protein | Nitric oxide synthase | Tetrahydrobiopterin
