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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Detalhes bibliográficos
Main Authors: Crane, B R, Rosenfeld, R J, Arvai, A S, Ghosh, D K, Ghosh, S, Tainer, J A, Stuehr, D J, Getzoff, E D
Formato: Artigo
Idioma:English
Publicado em: 1999
Assuntos:
Research Article
Acesso em linha: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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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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