Structure of Thermally Activated TRP Channels

被引:22
|
作者
Cohen, Matthew R. [1 ,2 ]
Moiseenkova-Bell, Vera Y. [1 ,2 ]
机构
[1] Case Western Reserve Univ, Sch Med, Dept Pharmacol, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH 44106 USA
来源
THERMAL SENSORS | 2014年 / 74卷
关键词
ANKYRIN REPEAT DOMAIN; ION-CHANNEL; TRANSMEMBRANE DOMAINS; CRYSTAL-STRUCTURE; CATION CHANNEL; CAPSAICIN-RECEPTOR; COLD SENSITIVITY; MOLECULAR-BASIS; PROTEIN; REVEALS;
D O I
10.1016/B978-0-12-800181-3.00007-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Temperature sensation is important for adaptation and survival of organisms. While temperature has the potential to affect all biological macromolecules, organisms have evolved specific thermosensitive molecular detectors that are able to transduce temperature changes into physiologically relevant signals. Among these thermosensors are ion channels from the transient receptor potential (TRP) family. Prime candidates include TRPV1-4, TRPA1, and TRPM8 (the so-called "thermoTRP" channels), which are expressed in sensory neurons and gated at specific temperatures. Electro-physiological and thermodynamic approaches have been employed to determine the nature by which thermoTRPs detect temperature and couple temperature changes to channel gating. To further understand how thermoTRPs sense temperature, high-resolution structures of full-length thermoTRPs channels will be required. Here, we will discuss current progress in unraveling the structures of thermoTRP channels.
引用
收藏
页码:181 / 211
页数:31
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