scholarly journals Structural basis of the transmembrane domain dimerization and rotation in the activation mechanism of the TRKA receptor by nerve growth factor

2019 ◽  
Vol 295 (1) ◽  
pp. 275-286 ◽  
Author(s):  
María L. Franco ◽  
Kirill D. Nadezhdin ◽  
Sergey A. Goncharuk ◽  
Konstantin S. Mineev ◽  
Alexander S. Arseniev ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Transmembrane Domain ◽  
Activation Mechanism ◽  
Structural Basis ◽  
Trka Receptor ◽  
Nerve Growth

Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor

Nature ◽  
10.1038/43705 ◽  
1999 ◽  
Vol 401 (6749) ◽  
pp. 184-188 ◽  
Author(s):  
Christian Wiesmann ◽  
Mark H. Ultsch ◽  
Steven H. Bass ◽  
Abraham M. de Vos
Keyword(s):  
Crystal Structure ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Trka Receptor ◽  
Nerve Growth

Immunoglobulin-like domains define the nerve growth factor binding site of the TrkA receptor

1997 ◽  
Vol 15 (7) ◽  
pp. 668-672 ◽  
Author(s):  
Paul H. Holden ◽  
Vipin Asopa ◽  
Alan G.S. Robertson ◽  
Anthony R. Clarke ◽  
Sue Tyler ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Binding Site ◽  
Trka Receptor ◽  
Nerve Growth ◽  
Factor Binding Site ◽  
Factor Binding

scholarly journals Nerve growth factor activation of the TrkA receptor induces cell death, by macropinocytosis, in medulloblastoma Daoy cells

2010 ◽  
Vol 112 (4) ◽  
pp. 882-899 ◽  
Author(s):  
Chunhui Li ◽  
James I. S. MacDonald ◽  
Todd Hryciw ◽  
Susan O. Meakin
Keyword(s):  
Cell Death ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Trka Receptor ◽  
Nerve Growth

scholarly journals The structure of nerve growth factor in complex with lysophosphatidylinositol

2015 ◽  
Vol 71 (7) ◽  
pp. 906-912 ◽  
Author(s):  
Han-Li Sun ◽  
Tao Jiang
Keyword(s):  
Crystal Structure ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Lipid Binding ◽  
Structural Basis ◽  
Recognition Mechanism ◽  
Nerve Growth ◽  
Physiological Processes ◽  
Dimeric Interface ◽  
Specific Lipid

Nerve growth factor (NGF) is an important protein that is involved in a variety of physiological processes in cell survival, differentiation, proliferation and maintenance. The previously reported crystal structure of mouse NGF (mNGF) in complex with lysophosphatidylserine (LysoPS) showed that mNGF can bind LysoPS at its dimeric interface. To expand the understanding of the structural basis for specific lipid recognition by NGF, the crystal structure of mNGF complexed with lysophosphatidylinositol (13:0 LysoPI) was solved. Interestingly, in addition to Lys88, which interacts with the head glycerol group and the phosphate group of LysoPI, as seen in the mNGF–LysoPS structure, two additional residues, Tyr52 and Arg50, were found to assist in lipid binding by forming hydrogen bonds to the inositol moiety of the LysoPI molecule. The results suggest a specific recognition mechanism of inositol group-containing lipids by NGF, which may help in the design of bioactive compounds that can be delivered by NGF.

scholarly journals The trkA Receptor Mediates Growth Cone Turning toward a Localized Source of Nerve Growth Factor

1997 ◽  
Vol 17 (14) ◽  
pp. 5445-5454 ◽  
Author(s):  
Gianluca Gallo ◽  
Frances B. Lefcort ◽  
Paul C. Letourneau
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Growth Cone ◽  
Trka Receptor ◽  
Nerve Growth ◽  
Localized Source
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