Abstract
We used a computer-based prediction algorithm to identify probable coiled-coil segments at the N-termini of G protein α, β and γ subunits. This result indicates that G protein trimers may form via a three-stranded coiled coil. Previous biochemical results had shown that the N-termini of α and β are involved in subunit interactions. Here we present a structural model for the N-terminal domain of βγ and a hypothesis for the reversible association of α to βγ.
Original language | English (US) |
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Pages (from-to) | 105-108 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 314 |
Issue number | 2 |
DOIs | |
State | Published - Dec 14 1992 |
All Science Journal Classification (ASJC) codes
- Genetics
- Molecular Biology
- Biophysics
- Structural Biology
- Biochemistry
- Cell Biology
Keywords
- Coiled coil
- G protein structure, Transducin βγ dimer
- G protein trimerization