Structure and function of the visual arrestin oligomer.
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ABSTRACT:
SUBMITTER: Hanson SM
PROVIDER: S-EPMC1829381 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
Publications
Structure and function of the visual arrestin oligomer.
Hanson Susan M SM Van Eps Ned N Francis Derek J DJ Altenbach Christian C Vishnivetskiy Sergey A SA Arshavsky Vadim Y VY Klug Candice S CS Hubbell Wayne L WL Gurevich Vsevolod V VV
The EMBO journal 20070301 6
A distinguishing feature of rod arrestin is its ability to form oligomers at physiological concentrations. Using visible light scattering, we show that rod arrestin forms tetramers in a cooperative manner in solution. To investigate the structure of the tetramer, a nitroxide side chain (R1) was introduced at 18 different positions. The effects of R1 on oligomer formation, EPR spectra, and inter-spin distance measurements all show that the structures of the solution and crystal tetramers are diff ...[more]
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