ロード中...
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...
保存先:
| 主要な著者: | , , , |
|---|---|
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Portland Press Ltd.
2005
|
| 主題: | |
| オンライン・アクセス: | 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 |
| タグ: |
タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!
|