Neurotransmitters: Difference between revisions

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Line 96:

**Noradrenaline

**Carmoterol, see [[2y02]].

**Salbutamol (Albuterol in USA), [[2y04]].

**[[Salbutamol]] (Albuterol in USA), [[2y04]].

*Beta blockers:

**Metoprolol

Line 114:

*Gs: adenylate cyclase activated, cAMP up. For Gs see [[Beta2 adrenergic receptor-Gs protein complex updated]].

β2-adrenergic agonists:

**Salbutamol (Albuterol in USA)

**[[Salbutamol]] (Albuterol in USA)

**Bitolterol mesylate

**Formoterol

**[[Formoterol]]

**Isoprenaline

**Levalbuterol

**Metaproterenol

**Salmeterol

**[[Salmeterol]]

**Terbutaline

**Ritodrine

Line 162:

=GABA=

==GABA receptors==

'''GABA''' (i.e. gamma-aminobutyric acid) is the primary inhibitory neurotransmitter of the vertebrate central nervous system. GABA can bind one of two different receptor proteins, each using a discrete mechanism to elicit a cellular response. Upon binding with GABA, '''GABAB receptors''' (metabotropic) utilize a second messenger amplification pathway that ultimately results in an inhibitory signal for neuronal transmission. This pathway for signal transmission differs from ~~'''~~GABAA receptors~~'''~~ (ionotropic), which are considered ligand-gated ion channels as the binding of GABA results in the opening of ion channels leading to the inhibition of a neuronal signal.

'''GABA''' (i.e. gamma-aminobutyric acid) is the primary inhibitory neurotransmitter of the vertebrate central nervous system. GABA can bind one of two different receptor proteins, each using a discrete mechanism to elicit a cellular response. Upon binding with GABA, '''GABAB receptors''' (metabotropic) utilize a second messenger amplification pathway that ultimately results in an inhibitory signal for neuronal transmission. This pathway for signal transmission differs from [[GABAA receptors]] (ionotropic), which are considered ligand-gated ion channels as the binding of GABA results in the opening of ion channels leading to the inhibition of a neuronal signal.

<scene name='82/829381/Cv/9'>GABA bound to the GABAB receptor</scene> (PDB code [[4ms3]]).

*[[GABA receptor]]

*[[User:Rana Saad/The human GABAb receptor]]

*[[GABAA receptor]]

==[[GABA(A) receptor-associated protein]]==

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Line 196:

<scene name='82/829381/Cv/5'>Histamine</scene>.

==Histamine receptors==

Allergy symptoms are mostly caused by the release of histamine in response to allergens. The binding of histamine to the extracellular portion of the H1 receptor triggers a structural change of the transmembrane portion, leading to a change in the C terminal area. This c terminal region interacts with G proteins, leading to the activation of the Gq signalling pathway, which triggers allergy symptoms like itchy eyes and runny noses. Many allergy drugs are anti-histamines, in that they bind to the histamine receptor but do not cause the conformational change that leads to a response. The H1 receptor is a histamine receptor belonging to the family of rhodopsin-like G-protein-coupled receptors. The H1 receptor is linked to an intracellular G-protein (Gq) that activates [[phospholipase C]] (see [[PLC beta 3 Gq|Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q]] and the inositol triphosphate (IP3) signalling pathway. When a ligand binds to a G protein-coupled ~~receptorthat~~ is coupled to a Gq heterotrimeric G protein, the α-subunit of Gq can bind to and induce activity in the PLC isozyme PLC-β, which results in the cleavage of PIP2 into IP3 and DAG.

Allergy symptoms are mostly caused by the release of histamine in response to allergens. The binding of histamine to the extracellular portion of the H1 receptor triggers a structural change of the transmembrane portion, leading to a change in the C terminal area. This c terminal region interacts with G proteins, leading to the activation of the Gq signalling pathway, which triggers allergy symptoms like itchy eyes and runny noses. Many allergy drugs are anti-histamines, in that they bind to the histamine receptor but do not cause the conformational change that leads to a response. The H1 receptor is a histamine receptor belonging to the family of rhodopsin-like G-protein-coupled receptors. The H1 receptor is linked to an intracellular G-protein (Gq) that activates [[phospholipase C]] (see [[PLC beta 3 Gq|Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q]] and the inositol triphosphate (IP3) signalling pathway. When a ligand binds to a G protein-coupled receptor that is coupled to a Gq heterotrimeric G protein, the α-subunit of Gq can bind to and induce activity in the PLC isozyme PLC-β, which results in the cleavage of PIP2 into IP3 and DAG.

*[[Histamine H1 receptor]]

* [[3rze]] - human histamine H1 receptor with an antagonist doxepin.

Line 205:

Line 206:

The ligand for NTSR1 is the 13 amino acid peptide, neurotensin (NTS)<ref name="SONT">PMID:23051748</ref>, and the majority of the effects of NTS are mediated through NTSR1<ref name="SONT"/>. NTS has a variety of biological activities including a role in the '''[https://en.wikipedia.org/wiki/Leptin leptin]''' signaling pathways <ref name="Mice">PMID: 20211191</ref>, tumor growth <ref name="cancer">PMID:16887236</ref>, and '''[https://en.wikipedia.org/wiki/Dopamine dopamine]''' regulation <ref name="Schizophrenia">PMID:22596253</ref>. NTSR1 was crystallized bound with a C-terminal portion of its tridecapeptide '''[https://en.wikipedia.org/wiki/Ligand ligand]''', <scene name='72/721548/Neurotensin/7'>NTS(8-13)</scene>. The shortened ligand was used because of oits higher potency and efficacy than its full-length counterpart<ref name="SONT"/>.

[[Neurotensin receptor]]

*[[Neurotensin receptor]]

Like other G protein-coupled receptors, NTSR1 is composed of 3 distinct regions. An <scene name='72/727765/Overall_structure/5'>extracellular binding site</scene> where neurotensin binds and causes a conformational change of the protein. A region containing <scene name='73/733990/Overall/1'>7 transmembrane alpha helices</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] that transduce the signal from the extracellular side of the cell membrane to the intracellular side. Lastly, an intracellular region that when activated by a conformational change in the protein activates a [https://en.wikipedia.org/wiki/G_protein G-protein] associated with this receptor.

The <scene name='72/721547/Hydrophobic_binding_pocket/6'>hydrophobic binding pocket</scene> in NTSR1 is located at the top of the protein (Figure 1). NTSR1 also contains an '''[https://en.wikipedia.org/wiki/Allosteric_regulation allosteric]''' <scene name='72/721548/Na_bind_pocket/13'>sodium binding pocket</scene>, which is located directly beneath the ligand binding pocket and the two pockets, which are separated by the residue <scene name='72/721548/Trp321/1'>Trp321</scene><ref name="SPGP">PMID:26205105</ref>. NTSR1 has been mutated to exist in both <scene name='72/721548/Ntsr1-elf/6'>active</scene> and <scene name='72/721547/Ntsr1-gw5/8'>active-like</scene> states.

=Serotonin=

Neurotransmitters: Difference between revisions

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@@ Line 96: / Line 96: @@
 **Noradrenaline
 **Carmoterol, see [[2y02]].
-**Salbutamol (Albuterol in USA), [[2y04]].
+**[[Salbutamol]] (Albuterol in USA), [[2y04]].
 *Beta blockers:
 **Metoprolol
@@ Line 114: / Line 114: @@
 *G<sub>s</sub>: adenylate cyclase activated, cAMP up. For G<sub>s</sub> see [[Beta2 adrenergic receptor-Gs protein complex updated]].
 β2-adrenergic agonists:
-**Salbutamol (Albuterol in USA)
+**[[Salbutamol]] (Albuterol in USA)
 **Bitolterol mesylate
-**Formoterol
+**[[Formoterol]]
 **Isoprenaline
 **Levalbuterol
 **Metaproterenol
-**Salmeterol
+**[[Salmeterol]]
 **Terbutaline
 **Ritodrine
@@ Line 162: / Line 162: @@
 =GABA=
 ==GABA receptors==
-'''GABA''' (i.e. gamma-aminobutyric acid) is the primary inhibitory neurotransmitter of the vertebrate central nervous system. GABA can bind one of two different receptor proteins, each using a discrete mechanism to elicit a cellular response. Upon binding with GABA, '''GABAB receptors''' (metabotropic) utilize a second messenger amplification pathway that ultimately results in an inhibitory signal for neuronal transmission. This pathway for signal transmission differs from '''GABAA receptors''' (ionotropic), which are considered ligand-gated ion channels as the binding of GABA results in the opening of ion channels leading to the inhibition of a neuronal signal.
+'''GABA''' (i.e. gamma-aminobutyric acid) is the primary inhibitory neurotransmitter of the vertebrate central nervous system. GABA can bind one of two different receptor proteins, each using a discrete mechanism to elicit a cellular response. Upon binding with GABA, '''GABAB receptors''' (metabotropic) utilize a second messenger amplification pathway that ultimately results in an inhibitory signal for neuronal transmission. This pathway for signal transmission differs from [[GABAA receptors]] (ionotropic), which are considered ligand-gated ion channels as the binding of GABA results in the opening of ion channels leading to the inhibition of a neuronal signal.
 <scene name='82/829381/Cv/9'>GABA bound to the GABAB receptor</scene> (PDB code [[4ms3]]).
 *[[GABA receptor]]
 *[[User:Rana Saad/The human GABAb receptor]]
+*[[GABAA receptor]]
 ==[[GABA(A) receptor-associated protein]]==
@@ Line 195: / Line 196: @@
 <scene name='82/829381/Cv/5'>Histamine</scene>.
 ==Histamine receptors==
-Allergy symptoms are mostly caused by the release of histamine in response to allergens. The binding of histamine to the extracellular portion of the H1 receptor triggers a structural change of the transmembrane portion, leading to a change in the C terminal area. This c terminal region interacts with G proteins, leading to the activation of the Gq signalling pathway, which triggers allergy symptoms like itchy eyes and runny noses. Many allergy drugs are anti-histamines, in that they bind to the histamine receptor but do not cause the conformational change that leads to a response. The H1 receptor is a histamine receptor belonging to the family of rhodopsin-like G-protein-coupled receptors. The H1 receptor is linked to an intracellular G-protein (G<sub>q</sub>) that activates [[phospholipase C]] (see [[PLC beta 3 Gq|Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q]] and the inositol triphosphate (IP3) signalling pathway. When a ligand binds to a G protein-coupled receptorthat is coupled to a G<sub>q</sub> heterotrimeric G protein, the α-subunit of G<sub>q</sub> can bind to and induce activity in the PLC isozyme PLC-β, which results in the cleavage of PIP2 into IP3 and DAG.
+Allergy symptoms are mostly caused by the release of histamine in response to allergens. The binding of histamine to the extracellular portion of the H1 receptor triggers a structural change of the transmembrane portion, leading to a change in the C terminal area. This c terminal region interacts with G proteins, leading to the activation of the Gq signalling pathway, which triggers allergy symptoms like itchy eyes and runny noses. Many allergy drugs are anti-histamines, in that they bind to the histamine receptor but do not cause the conformational change that leads to a response. The H1 receptor is a histamine receptor belonging to the family of rhodopsin-like G-protein-coupled receptors. The H1 receptor is linked to an intracellular G-protein (G<sub>q</sub>) that activates [[phospholipase C]] (see [[PLC beta 3 Gq|Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q]] and the inositol triphosphate (IP3) signalling pathway. When a ligand binds to a G protein-coupled receptor that is coupled to a G<sub>q</sub> heterotrimeric G protein, the α-subunit of G<sub>q</sub> can bind to and induce activity in the PLC isozyme PLC-β, which results in the cleavage of PIP2 into IP3 and DAG.
 *[[Histamine H1 receptor]]
 * [[3rze]] - human histamine H1 receptor with an antagonist doxepin.
@@ Line 205: / Line 206: @@
 The ligand for NTSR1 is the 13 amino acid peptide, neurotensin (NTS)<ref name="SONT">PMID:23051748</ref>, and the majority of the effects of NTS are mediated through NTSR1<ref name="SONT"/>. NTS has a variety of biological activities including a role in the '''[https://en.wikipedia.org/wiki/Leptin leptin]''' signaling pathways <ref name="Mice">PMID: 20211191</ref>, tumor growth <ref name="cancer">PMID:16887236</ref>, and '''[https://en.wikipedia.org/wiki/Dopamine dopamine]''' regulation <ref name="Schizophrenia">PMID:22596253</ref>. NTSR1 was crystallized bound with a C-terminal portion of its tridecapeptide '''[https://en.wikipedia.org/wiki/Ligand ligand]''', <scene name='72/721548/Neurotensin/7'>NTS(8-13)</scene>. The shortened ligand was used because of oits higher potency and efficacy than its full-length counterpart<ref name="SONT"/>.
-[[Neurotensin receptor]]
+*[[Neurotensin receptor]]
+Like other G protein-coupled receptors, NTSR1 is composed of 3 distinct regions. An <scene name='72/727765/Overall_structure/5'>extracellular binding site</scene> where neurotensin binds and causes a conformational change of the protein. A region containing <scene name='73/733990/Overall/1'>7 transmembrane alpha helices</scene> (PDB code:[http://www.rcsb.org/pdb/explore/explore.do?structureId=4GRV 4GRV)] that transduce the signal from the extracellular side of the cell membrane to the intracellular side. Lastly, an intracellular region that when activated by a conformational change in the protein activates a [https://en.wikipedia.org/wiki/G_protein G-protein] associated with this receptor.
+The <scene name='72/721547/Hydrophobic_binding_pocket/6'>hydrophobic binding pocket</scene> in NTSR1 is located at the top of the protein (Figure 1). NTSR1 also contains an '''[https://en.wikipedia.org/wiki/Allosteric_regulation allosteric]''' <scene name='72/721548/Na_bind_pocket/13'>sodium binding pocket</scene>, which is located directly beneath the ligand binding pocket and the two pockets, which are separated by the residue <scene name='72/721548/Trp321/1'>Trp321</scene><ref name="SPGP">PMID:26205105</ref>. NTSR1 has been mutated to exist in both <scene name='72/721548/Ntsr1-elf/6'>active</scene> and <scene name='72/721547/Ntsr1-gw5/8'>active-like</scene> states.
 =Serotonin=