Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching.
A more global search method, using fewer assumptions, has been used to predict the structure of the dimeric transmembrane region of the protein glycophorin A. The resulting model significantly differs from that previously determined. In particular, the arrangement between the two transmembrane helices is now more symmetric resulting in improved interaction energies and an increased buried surface area. An increase in the van der Waals interaction energy due to tighter packing compensates for the loss of the interhelical hydrogen bond observed between Thr-87 of each helix in the previous model.
Adams
P D
PD
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
Engelman
D M
DM
Brünger
A T
AT
D003198:Computer Simulation; D019281:Dimerization; D005544:Forecasting; D006021:Glycophorins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular
D006021:Glycophorins; D008565:Membrane Proteins