The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function

The common fold shared by members of the glutathione-transferase (GST) family has a topologically conserved isoleucine residue at the N-terminus of helix 3 which is involved in the packing of helix 3 against two β-strands in domain 1. The role of the isoleucine residue in the structure, function and...

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Autores principales: Achilonu, Ikechukwu, Gildenhuys, Samantha, Fisher, Loren, Burke, Jonathan, Fanucchi, Sylvia, Sewell, B. Trevor, Fernandes, Manuel, Dirr, Heini W.
Formato: Artigo
Lenguaje:Inglês
Publicado: International Union of Crystallography 2010
Materias:
Structural Communications
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC2898459/
https://ncbi.nlm.nih.gov/pubmed/20606271
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309110019135
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