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'''IL-36'''  acts on naïve CD4+ T cells.<br />
'''IL-36'''  acts on naïve CD4+ T cells.<br />
''' IL-37''' has a role in inhibiting both innate and adaptive immune responses.<br />
''' IL-37''' has a role in inhibiting both innate and adaptive immune responses.<br />
*[[Neurotrophin]]
*[[High affinity nerve growth factor receptor]]
'''TrkA'''. Trk stands for Topomyosin-Related Kinase. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation. <scene name='80/805001/Cv/4'>Structure of Nerve Growth Factor Complexed with the Extracellular Domain of TrkA</scene>. An <scene name='80/805001/Cv/7'>Arg residue</scene>, conserved in all neutrophins, forms the most important binding determinant between TrkA and its ligand - nerve growth factor - which forms the active homodimer of the receptor. <scene name='80/805001/Cv/6'>All interactions between TrkA chain A and NGF</scene>.
*[[Tyrosine kinase receptor|Tyrosine kinase receptor TrkA]]
TRK-A contains an extracellular ligand binding domain (LBD), a transmembrane helix and an intracellular region which contains the kinase domain. The kinase domain ([[4yne]]) contains the tripeptide DFG which flips out in TRK-A inactivated form. <scene name='83/839914/Cv/7'>Inhibitor binding site</scene> ([[4yne]]). The structure of the complex of TRK-A with the phenylpyrrolidine derivative shows the inhibitor forming hydrogen bonds to Met620 and Lys572 residues and π-π interactions of it with Phe617 and Phe 698.
The <scene name='83/839914/Cv/4'>complex between TRK-A and the nerve growth factor</scene> ([[2ifg]]) is a 2:2 dimer. The C-terminal immunoglobulin-like domain interacts with the NGF. The extracellular domain of TRK-A contains <scene name='83/839914/Cv/5'>3 Leu-rich regions</scene> flanked by  <scene name='83/839914/Cv/6'>Cys-rich regions</scene> (in yellow), 2 immunoglobulin-like domains and the nerve growth factor (NGF) binding domain.
*[[Neurotrophin|Neurotrophin & its receptor]]
*[[Neurotrophin|Neurotrophin & its receptor]]
The complex between NT3 and p75 neurotrophin receptor (p75NTR) shows a <scene name='80/805035/Cv/2'>homodimer of NT3 with two symmetrically arranged p75NTR molecules</scene>. There are 3 sites of interactions between NT3 and p75NTR - site 1, site 2 and site 3.
The complex between NT3 and p75 neurotrophin receptor (p75NTR) shows a <scene name='80/805035/Cv/2'>homodimer of NT3 with two symmetrically arranged p75NTR molecules</scene>. There are 3 sites of interactions between NT3 and p75NTR - site 1, site 2 and site 3.
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<scene name='80/805035/Cv/4'>Site 2</scene>.
<scene name='80/805035/Cv/4'>Site 2</scene>.


<scene name='80/805035/Cv/5'>Site 3</scene>.   
<scene name='80/805035/Cv/5'>Site 3</scene>.
 
[[High affinity nerve growth factor receptor]]
 
'''TrkA'''. Trk stands for Topomyosin-Related Kinase. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation. <scene name='80/805001/Cv/4'>Structure of Nerve Growth Factor Complexed with the Extracellular Domain of TrkA</scene>. An <scene name='80/805001/Cv/7'>Arg residue</scene>, conserved in all neutrophins, forms the most important binding determinant between TrkA and its ligand - nerve growth factor - which forms the active homodimer of the receptor. <scene name='80/805001/Cv/6'>All interactions between TrkA chain A and NGF</scene>.
 
[[Tyrosine kinase receptor|Tyrosine kinase receptor TrkA]]
 
TRK-A contains an extracellular ligand binding domain (LBD), a transmembrane helix and an intracellular region which contains the kinase domain. The kinase domain ([[4yne]]) contains the tripeptide DFG which flips out in TRK-A inactivated form. <scene name='83/839914/Cv/7'>Inhibitor binding site</scene> ([[4yne]]). The structure of the complex of TRK-A with the phenylpyrrolidine derivative shows the inhibitor forming hydrogen bonds to Met620 and Lys572 residues and π-π interactions of it with Phe617 and Phe 698.
 
The <scene name='83/839914/Cv/4'>complex between TRK-A and the nerve growth factor</scene> ([[2ifg]]) is a 2:2 dimer. The C-terminal immunoglobulin-like domain interacts with the NGF. The extracellular domain of TRK-A contains <scene name='83/839914/Cv/5'>3 Leu-rich regions</scene> flanked by <scene name='83/839914/Cv/6'>Cys-rich regions</scene> (in yellow), 2 immunoglobulin-like domains and the nerve growth factor (NGF) binding domain.
 
[[TrkB tyrosine kinase receptor]]
 
<scene name='80/805008/Cv/6'>Structure of the TrkB-d5:NT-4/5 Complex, comprising one homodimer of NT-4/5 bound to two monomers of TrkB-d5</scene>. TrkB and neutrotrophin-4/5 interact via a <scene name='80/805008/Cv/7'>specificity interaction site</scene> and via a <scene name='80/805008/Cv/8'>conserved interaction site</scene>.


*[[TrkB tyrosine kinase receptor]]
<scene name='80/805008/Cv/6'>Structure of the TrkB-d5:NT-4/5 Complex, comprising one homodimer of NT-4/5 bound to two monomers of TrkB-d5</scene>. TrkB and neutrotrophin-4/5 interact via a <scene name='80/805008/Cv/7'>specificity interaction site</scene> and via a <scene name='80/805008/Cv/8'>conserved interaction site</scene>
*[[Platelet-derived growth factors and receptors]]. Platelet-derived growth factor receptor belongs to [[Receptor tyrosine kinases]], class III.
*[[Platelet-derived growth factors and receptors]]. Platelet-derived growth factor receptor belongs to [[Receptor tyrosine kinases]], class III.
*[[Renalase]] (RNLS) – Anti-apoptotic survival factor
*[[Renalase]] (RNLS) – Anti-apoptotic survival factor

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Alexander Berchansky
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