期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 8, 期 32, 页码 3692-3706出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/b606019f
关键词
-
资金
- NCRR NIH HHS [5-P41-RR05969] Funding Source: Medline
- NIGMS NIH HHS [R01-GM073655] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR005969] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM073655] Funding Source: NIH RePORTER
Mechanical forces play an essential role in cellular processes as input, output, and signals. Various protein complexes in the cell are designed to handle, transform and use such forces. For instance, proteins of muscle and the extracellular matrix can withstand considerable stretching forces, hearing-related and mechanosensory proteins can transform weak mechanical stimuli into electrical signals, and regulatory proteins are suited to forcing DNA into loops to control gene expression. Here we review the structure - function relationship of four protein complexes with well defined and representative mechanical functions. The first example is titin, a protein that confers passive elasticity on muscle. The second system is the elastic extracellular matrix protein, fibronectin, and its cellular receptor integrin. The third protein system is the transduction apparatus in hearing and other mechanical senses, likely containing cadherin and ankyrin repeats. The last system is the lac repressor protein, which regulates gene expression by looping DNA. This review focuses on atomic level descriptions of the physical mechanisms underlying the various mechanical functions of the stated proteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据