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N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization.
Nitric oxide synthase oxygenase domains (NOS(ox)) must bind tetrahydrobiopterin and dimerize to be active. New crystallographic structures of inducible NOS(ox) reveal that conformational changes in a switch region (residues 103-111) preceding a pterin-binding segment exchange N-terminal beta-hairpin...
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| Huvudupphovsmän: | , , , , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1999
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1171690/ https://ncbi.nlm.nih.gov/pubmed/10562539 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.22.6271 |
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