ArticleBiophysical journal2005
Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Discovering immunoreceptor coupling and organization motifs.Frontiers in immunology · 2023Article
- Solid state deuterium NMR study of LKα14 peptide aggregation in biosilica.Biointerphases · 2017Article
- His499 Regulates Dimerization and Prevents Oncogenic Activation by Asparagine Mutations of the Human Thrombopoietin Receptor.The Journal of biological chemistry · 2016Article
- Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3.Biochemistry · 2014Article
- Tryptophan at the transmembrane-cytosolic junction modulates thrombopoietin receptor dimerization and activation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance.Biochemistry · 2010Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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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Registered trials
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