| Autor: |
Fischmann, Thierry O., Hruza, Alan, Niu, Xiao Da, Fossetta, James D., Lunn, Charles A., Dolphin, Edward, Prongay, Andrew J., Reichert, Paul, Lundell, Daniel J., Narula, Satwant K., Weber, Patricia C. |
| Předmět: |
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| Zdroj: |
Nature Structural Biology; Mar1999, Vol. 6 Issue 3, p233, 10p |
| Abstrakt: |
Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 Å resolution) and iNOS (2.25 Å resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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