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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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| Huvudupphovsmän: | , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Portland Press Ltd.
2005
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| Ämnen: | |
| Länkar: | 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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