糖抗生素的合作结合相互作用
Hideyuki Shiozawa1, Brian C S Chia, Nichola L Davies
1Cambridge Center for Molecular Recognition, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Journal of the American Chemical Society
|April 11, 2002
概括
像chloroeremomycin这样的糖类抗生素在与细胞壁前体结合时会收紧它们的结构. 这种积极的合作是理解它们抗生素功能的关键.
科学领域:
- 生物化学 生物化学
- 微生物学 微生物学
- 结构生物学 结构生物学
背景情况:
- 糖类抗生素,如万科米,对于对抗细菌感染至关重要.
- 这些抗生素通常与细菌细胞壁前体结合,形成二极体.
- 这些结合事件与二聚体形成之间的相互作用尚未完全理解.
研究的目的:
- 调查糖抗生素中的联结和二聚体形成之间的相互作用.
- 阐明在抗生素二聚体接口上结合联体的结构后果.
- 探索在糖-连接体相互作用中积极合作的概念.
主要方法:
- 研究了因多尔-2-碳酸 (L) 与糖类抗生素chloroeremomycin (CE) 的结合.
- 分析了连接体和抗生素之间的结模式,并将它们与自然结合点进行比较.
- 研究了在甲胺素的二元界面上的结构变化,在结合器结合时.
主要成果:
- 印醇-2-碳素酸与甲素形成键,模仿自然的N-Ac-D-Ala结合.
- 联体对甲二元体的结合 (L/CE/CE/L) 会产生积极的合作性.
- 在联体诱导的正合作性后,在二元接口上观察到结构收紧.
结论:
- 联体结合诱导了糖抗生素二聚体中的积极合作性.
- 在二度接口的结构收紧是这种合作的关键后果.
- 这些发现提供了对万科米组抗生素的作用机制的见解.
相关概念视频
Drug-Receptor Bonds
5.1K
Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
In...
5.1K
Cooperative Binding of Transcription Regulators
7.4K
Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.4K
Cooperative Binding of Transcription Regulators
2.6K
No description available
2.6K
Cooperative Allosteric Transitions
9.1K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
9.1K
Cooperative Allosteric Transitions
2.7K
No description available
2.7K
Noncovalent Attractions in Biomolecules
65.7K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
65.7K


