期刊论文详细信息
FEBS Letters | |
The glycine‐rich loop of adenylate kinase forms a giant anion hole | |
Dreusicke, Dirk1  Schulz, Georg E.1  | |
[1] Institut für Organische Chemie und Biochemie der Universität, Albertstr. 21, 7800 Freiburg i.Br. FRG | |
关键词: Adenylate kinase X-ray diffraction Structural homology Nucleotide-binding protein Oncogene; | |
DOI : 10.1016/0014-5793(86)81037-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The conformation of the glycine-rich loop of adenylate kinase is described in detail. It forms a giant anion hole for a sulfate ion, which presumably mimicks a nucleotide phosphoryl group. This loop had been called flexible, because at pH values of 6 or below it is displaced in the crystal. In the region of this loop the adenylate kinases are probably homologous to the p21 proteins. Is is known that a mutation in this loop at residue 12 of p21 causes cell transformation and therefore cancer. Other potentially homologous proteins are indicated.
【 授权许可】
Unknown
【 预 览 】
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