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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...
Tallennettuna:
| Päätekijät: | , , , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
International Union of Crystallography
2010
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| Aiheet: | |
| Linkit: | 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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