期刊
JOURNAL OF GENERAL PHYSIOLOGY
卷 133, 期 3, 页码 231-237出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.200810137
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- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM081340] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM081340-02, R01 GM081340] Funding Source: Medline
Understanding how proteins facilitate signaling and substrate transport across biological membranes is an important frontier of structural biology. Membrane proteins are the doors and windows of cells: many membrane proteins are gates of entry into or exit from cells or cellular compartments, and others allow cells to sense their environment. One important multifunctional family of membrane proteins is the transient receptor potential (TRP) family of ion channels. TRP channels have recently been the subject of multiple structural analyses, both low resolution electron microscopy studies (reviewed by Moiseenkova-Bell and Wensel in this issue [p. 239]) and the divide and conquer approach of determining high resolution crystal structures of channel fragments, reviewed here.
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