2nsi: Difference between revisions

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[[Image:2nsi.gif|left|200px]]
{{Seed}}
[[Image:2nsi.png|left|200px]]


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{{STRUCTURE_2nsi|  PDB=2nsi  |  SCENE=  }}  
{{STRUCTURE_2nsi|  PDB=2nsi  |  SCENE=  }}  


'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-FREE, SEITU COMPLEX'''
===HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-FREE, SEITU COMPLEX===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10409685}}


==About this Structure==
==About this Structure==
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[[Category: Nitric oxide synthase]]
[[Category: Nitric oxide synthase]]
[[Category: Tetrahydrobiopterin]]
[[Category: Tetrahydrobiopterin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:49:27 2008''

Revision as of 07:49, 28 July 2008

File:2nsi.png

Template:STRUCTURE 2nsi

HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-FREE, SEITU COMPLEX

Template:ABSTRACT PUBMED 10409685

About this Structure

2NSI 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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