PDB | 2k1l NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 6.3
NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 6.3
label Keywords
epha1, receptor tyrosine kinase, dimeric transmembrane domain, atp-binding, glycoprotein, nucleotide-binding, phosphoprotein, polymorphism, transferase, tyrosine-protein kinase, signaling protein
event_note Published
05/29/2024
filter_center_focus Method
SOLUTION NMR
add_circle Ligands
Original publication
import_contacts Title
Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1.
import_contacts Journal
J.Biol.Chem. 2008
import_contacts DOI
10.1074/jbc.M803089200
person Authors
Schulga, A.A., Goncharuk, M.V., Artemenko, E.O., Arseniev, A.S., Volynsky, P.E., Bocharov, E.V., Ermolyuk, Y.S., Mayzel, M.L., Efremov, R.G.
Member of
copyrightData provided by Research Collaboration for Structural Biology, Schulga, A.A., Goncharuk, M.V., Artemenko, E.O., Arseniev, A.S., Volynsky, P.E., Bocharov, E.V., Ermolyuk, Y.S., Mayzel, M.L., Efremov, R.G. , provided free of copyright via the Protein DataBank. View original data or read license terms.
