Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus

Liu, Wei;Crocker, Evan;Constantinescu, Stefan;Smith, Steven O.
(2005) Biophysical Journal — Vol. 89, n° 2, p. 1194-1202 (2005)

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Abstract
gp55- P is a dimeric membrane protein with a single transmembrane helix that is coded by the env gene of the polycythemic strain of the spleen focus forming virus. gp55- P activates the erythropoietin ( Epo) receptor through specific transmembrane helix interactions, leading to Epo- independent growth of erythroid progenitors and eventually promoting erythroleukemia. We describe the use of magic angle spinning deuterium NMR to establish the structure of the transmembrane dimer of gp55- P in model membranes. Comparison of the deuterium lineshapes of leucines in the center ( Leu(396 - 399)) and at the ends ( Leu(385), Leu(407)) of the transmembrane sequence shows that gp55- P has a right- handed crossing angle with Leu(399) packed in the dimer interface. We discuss the implications of the structure of the gp55- P transmembrane dimer for activation of the Epo receptor.
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Liu, W., Crocker, E., Constantinescu, S., & Smith, S. O. (2005). Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus. Biophysical Journal, 89(2), 1194-1202. https://doi.org/10.1529/biophysj.104.057844 (Original work published 2005)