The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met(51) and Phe(52) in function and dimer stability

The dimeric structure of certain cytosolic GSTs (glutathione S-transferases) is stabilized by a hydrophobic lock-and-key motif at their subunit interface. In hGSTA1-1 (human class Alpha GST with two type-1 subunits), the key consists of two residues, Met(51) and Phe(52), that fit into a hydrophobic...

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Autores principales: Alves, Carla S., Kuhnert, Diane C., Sayed, Yasien, Dirr, Heini W.
Formato: Artigo
Lenguaje:Inglês
Publicado: Portland Press Ltd. 2005
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1360702/
https://ncbi.nlm.nih.gov/pubmed/16190865
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20051066
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