Document Type
Other
Publication Date
2023
Department
Department of Biological Sciences
Additional Department
Department of Computer Science
Abstract
Structural models for the ETR1 homodimer were generated with AlphaFold-Multimer. Coppers were modeled under two potential coordinations involving Cys65 and His69 of the ETR1 homodimer, one in which the two coppers are bound independently and do not share an interaction with each other, and another where they are closely bonded.
See the following publication for details: Azhar, B.J., Abbas, S., Aman, S., Yamburenko, M.V., Chen, W., Müller, L., Uzun, B., Jewell, D.A., Dong, J., Shakeel, S.N., Groth, G., Binder, B.M., Grigoryan, G., Schaller, G.E. (2023) Basis for high-affinity ethylene binding by the ethylene receptor ETR1 of Arabidopsis. Proc. Natl. Acad. Sci. USA. 120:e2215195120. doi: 10.1073/pnas.2215195120
Dartmouth Digital Commons Citation
Azhar, Beenish J.; Abbas, Safdar; Aman, Sitwat; Yamburenko, Maria V.; Chen, Wei; Muller, Lena; Uzun, Buket; Jewell, David A.; Dong, Jian; Shakeel, Samina N.; Groth, Georg; Binder, Brad M.; Grigoryan, Gevorg; and Schaller, G. Eric, "Structural Files for the ETR1 Ethylene-Receptor Dimer Based on Computational Modeling" (2023). Dartmouth Scholarship. 4313.
https://digitalcommons.dartmouth.edu/facoa/4313
Supplement 1: PDB file for ETR1_AlphaFoldDimer_Cu_interacting
ETR1_AlphaFoldDimer_CU_notinteracting.pdb (916 kB)
Supplement 2: PDB file for ETR1_AlphaFoldDimer_CU_notinteracting
ETR1_AlphafoldDimer.pse (6795 kB)
Supplement 3: PyMOL file for ETR1_AlphaFoldDimer