Abstract:
:X-ray crystallography has made considerable recent progress in providing static structures of ion channels. Here we describe a complementary method-systematic fluorescence scanning-that reveals the structural dynamics of a channel. Local protein motion was measured from changes in the fluorescent intensity of a fluorophore attached at one of 37 positions in the pore domain and in the S4 voltage sensor of the Shaker K+ channel. The local rearrangements that accompany activation and slow inactivation were mapped onto the homologous structure of the KcsA channel and onto models of S4. The results place clear constraints on S4 location, voltage-dependent movement, and the mechanism of coupling of S4 motion to the operation of the slow inactivation gate in the pore domain.
journal_name
Neuronjournal_title
Neuronauthors
Gandhi CS,Loots E,Isacoff EYdoi
10.1016/s0896-6273(00)00068-4subject
Has Abstractpub_date
2000-09-01 00:00:00pages
585-95issue
3eissn
0896-6273issn
1097-4199pii
S0896-6273(00)00068-4journal_volume
27pub_type
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