1nsi: Difference between revisions
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[[Image:1nsi.gif|left|200px]] | [[Image:1nsi.gif|left|200px]] | ||
'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX''' | {{Structure | ||
|PDB= 1nsi |SIZE=350|CAPTION= <scene name='initialview01'>1nsi</scene>, resolution 2.55Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NSI is a [ | 1NSI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10409685 10409685] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Nitric-oxide synthase]] | [[Category: Nitric-oxide synthase]] | ||
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[[Category: tetrahydrobiopterin]] | [[Category: tetrahydrobiopterin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:05 2008'' | ||
Revision as of 11:01, 20 March 2008
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| 1nsi, resolution 2.55Å | |||||||||||||
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| Ligands: | SO4, ZN, HEM, H4B, ARG and GOL | ||||||||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX
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. 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
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