1nsi

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Revision as of 16:18, 12 November 2007

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spinqualitylabelsall models 1nsi, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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 SO4, ZN, HEM, H4B, ARG and GOL 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

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