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The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices.
- Source :
-
Biochemistry [Biochemistry] 1992 Dec 29; Vol. 31 (51), pp. 12726-32. - Publication Year :
- 1992
-
Abstract
- Recent studies suggest specific roles for transmembrane helix association in a range of functions, but understanding of the conformation and energetics of these interactions has been elusive. We have studied the specific dimerization of the transmembrane helix of glycophorin A by calculating the minimized interaction energies of a large number of conformations using simulated annealing techniques and tested the models against mutational analysis data. We find that the dimer is best modeled as a right-handed supercoil with an extensive region of close packing along the dimer interface. Furthermore, we observe a sequence-specific propensity for a right-handed supercoil to form when starting the simulated annealing modeling from a dimer of helices with parallel axes, in contrast with the dimerization region of the transcription factor GCN4 which shows a high propensity for the more prevalent left-handed supercoiling.
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 31
- Issue :
- 51
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1463744
- Full Text :
- https://doi.org/10.1021/bi00166a003