Solution NMR studies of integral polytopic a-helical membrane proteins: the structure determination of the seven-helix transmembrane receptor sensory rhodopsin II, pSRII.
Solution NMR studies of integral polytopic a-helical membrane proteins: the structure determination of the seven-helix transmembrane receptor sensory rhodopsin II, pSRII.
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整体多面α螺旋膜蛋白的溶液核磁共振研究:七螺旋跨膜受体感觉视紫红质II,pSRII的结构测定。
DOI:
10.1007/978-1-62703-023-6_3
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Gautier A
中科院分区:
文献类型:
--
作者:
Gautier A
About 30% of the proteins encoded in the genome are expressed as membrane proteins but these represent <1% of all the structures solved today. In view of the physiological and pharmaceutical significance of membrane proteins it is clear that a better and more comprehensive understanding of their three-dimensional (3D) structures at atomic resolution is required. α-Helical integral membrane proteins are generally more difficult to work with than β-barrel-type proteins and this has particularly been true for the polytopic members such as the large family of seven-helical proteins. In this chapter we describe the practical aspects of the solution-state NMR spectroscopy structure determination of the seven-helical transmembrane (7-TM) protein receptor sensory rhodopsin pSRII from the haloalkaliphilic archaeonNatronomonas pharaonisreconstituted in detergent micelles. This is the first time that a three-dimensional structure of a 7-TM protein has been determined by NMR.