| Molecular Modeling of Interactions of the Benzolactam-V8 Modulators with the Cys2 Domain of Protein Kinase Cδ |
| |
| 引用本文： | 黄莉莉 马大为 夏宗芗. Molecular Modeling of Interactions of the Benzolactam-V8 Modulators with the Cys2 Domain of Protein Kinase Cδ[J]. 中国化学, 2007, 25(10): 1434-1438. DOI: 10.1002/cjoc.200790265 |
| |
| 作者姓名： | 黄莉莉 马大为 夏宗芗 |
| |
| 作者单位： | State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China |
| |
| 基金项目： | Project supported by the National Natural Science Foundation of China （No. 30370335）. |
| |
| 摘 要： | Molecular modeling of interactions of four 7- or 8-substituted benzolactam-V8 （BLV） molecules with the cys2 activator-binding domain of protein kinase C （PKCδ） was carried out using molecular docking program Autodock. The docked models reveal that the hydroxymethyl group at the C（5） atom of the eight-membered ring of each BLV is bound at the bottom of the binding groove of the cys2 domain of PKCδ The BLV molecules make hydrogen bonds and hydrophobic interactions with PKCδ, which are similar to those in the crystal structure of the cys2 domain of PKCδ in complex with phorbol 13-acetate. BLV-1 does not contain a long side chain that is hydrophobic and necessary for membrane insertion, so that it would not be a potent modulator of PKCδ. The other three BLV molecules have long side chains substituted at C（7） or C（8） atoms, and it was predicted, based on the docking results, that they had the PKCδ-binding affinity in the order of BLV-2〉BLV-4〉BLV-3, and BLV-2 would be a potent activator of PKCδ.
|
| 关 键 词： | 蛋白激酶 调制器 分子模型 氢键 |
| 修稿时间： | 2007-02-15 |
Molecular Modeling of Interactions of the Benzolactam‐V8 Modulators with the Cys2 Domain of Protein Kinase Cδ |
| |
| HUANG, Li-Li MA, Da-Wei XIA, Zong-Xiang. Molecular Modeling of Interactions of the Benzolactam‐V8 Modulators with the Cys2 Domain of Protein Kinase Cδ[J]. Chinese Journal of Chemistry, 2007, 25(10): 1434-1438. DOI: 10.1002/cjoc.200790265 |
| |
| Authors: | HUANG Li-Li MA Da-Wei XIA Zong-Xiang |
| |
| Affiliation: | State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China |
| |
| Abstract: | Molecular modeling of interactions of four 7‐ or 8‐substituted benzolactam‐V8 (BLV) molecules with the cys2 activator‐binding domain of protein kinase C (PKCδ) was carried out using molecular docking program Autodock. The docked models reveal that the hydroxymethyl group at the C(5) atom of the eight‐membered ring of each BLV is bound at the bottom of the binding groove of the cys2 domain of PKCδ. The BLV molecules make hydrogen bonds and hydrophobic interactions with PKCδ, which are similar to those in the crystal structure of the cys2 domain of PKCδ in complex with phorbol 13‐acetate. BLV‐1 does not contain a long side chain that is hydrophobic and necessary for membrane insertion, so that it would not be a potent modulator of PKCδ. The other three BLV molecules have long side chains substituted at C(7) or C(8) atoms, and it was predicted, based on the docking results, that they had the PKCδ‐binding affinity in the order of BLV‐2>BLV‐4>BLV‐3, and BLV‐2 would be a potent activator of PKCδ. |
| |
| Keywords: | protein kinase regulatory domain modulator benzolactam molecular docking protein‐ligand interaction hydrogen bond hydrophobic interaction PKCδ‐binding affinity |
| 本文献已被 维普 等数据库收录！ |
