C-terminal peptides of rhodopsin. Determination of the optimum sequence for recognition of retinal transducin.

C-terminal peptides of rhodopsin. Determination of the optimum sequence for recognition of retinal transducin.
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视紫红质的 C 端肽。

DOI:
10.1042/bj2350309
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发表时间:
1986
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Takemoto,LJ
Takemoto,LJ
中科院分区:
--
文献类型:
--
作者:
Takemoto,DJ;Morrison,D;Davis,LC;Takemoto,LJ

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In vertebrate retinal rod outer segments, transducin, a guanine-nucleotide-binding protein, mediates signal coupling between rhodopsin and cyclic GMP phosphodiesterase. Whereas the T alpha subunit (39 kDa) of transducin binds guanine nucleotides and is the activator of the phosphodiesterase, the T beta gamma subunits (35 and 10 kDa) may function to physically link T alpha with photolysed rhodopsin. We have previously reported that a site of binding of transducin is on the C-terminus of bovine rhodopsin. By using competition with synthetic peptides, the recognition region was localized to bovine opsin amino acid residues 317-339. Further studies are detailed which determine the boundaries of this binding site on rhodopsin, as well as some of the critical amino acids needed for transducin binding. These results suggest that the serine and threonine residues in the rhodopsin C-terminal peptides Rhod-1 and Rhod-3 are critical for reconstitution of transducin GTPase activity.
DOI: --
发表时间: 1988
期刊: AJNR. American journal of neuroradiology
影响因子: --
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DOI: --
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