Histamine H1 receptor: Difference between revisions

Revision as of 21:37, 6 April 2018

Histamine H1 ReceptorHistamine H1 Receptor

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 eyeys 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.

Structural highlights

The structure of the H1 histamine receptor bound to an antihistamine, doxepin was published in 2011 ^[1]. A view colors the N terminus blue and the C terminus red, with the intervening segments paralleling the rainbow (blue, green, yellow, orange, red). This image is oriented with the transmembrane section at the top and the cytosolic portion below.

binds among the transmembrane alpha helices. Binding is stabilized by a number of . Interestingly, second generation antihistamines take advantage of an anion binding site formed by ; in this structure, they interact with a phosphate.

ReferencesReferences

↑ Shimamura T, Shiroishi M, Weyand S, Tsujimoto H, Winter G, Katritch V, Abagyan R, Cherezov V, Liu W, Han GW, Kobayashi T, Stevens RC, Iwata S. Structure of the human histamine H1 receptor complex with doxepin. Nature. 2011 Jun 22;475(7354):65-70. doi: 10.1038/nature10236. PMID:21697825 doi:10.1038/nature10236

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Michal Harel, Alexander Berchansky

[1] Shimamura T, Shiroishi M, Weyand S, Tsujimoto H, Winter G, Katritch V, Abagyan R, Cherezov V, Liu W, Han GW, Kobayashi T, Stevens RC, Iwata S. Structure of the human histamine H1 receptor complex with doxepin. Nature. 2011 Jun 22;475(7354):65-70. doi: 10.1038/nature10236. PMID:21697825 doi:10.1038/nature10236

[1]

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 == Structural highlights ==
-The structure of the H1 histamine receptor bound to an antihistamine, doxepin was published in 2011 <ref>PMID:21697825</ref>.
+The structure of the H1 histamine receptor bound to an antihistamine, doxepin was published in 2011 <ref>PMID:21697825</ref>. A <scene name='78/784820/N_to_c_rainbow/1'>N-->C rainbow</scene> view colors the N terminus blue and the C terminus red, with the intervening segments paralleling the rainbow (blue, green, yellow, orange, red).  This image is oriented with the transmembrane section at the top and the cytosolic portion below.
+<scene name='78/784820/Doxepin/2'>Doxepin</scene> binds among the transmembrane alpha helices.  Binding is stabilized by a number of <scene name='78/784820/Interacting_amino_acids/1'>interactions with amino acids</scene>.  Interestingly, second generation antihistamines take advantage of an anion binding site formed by <scene name='78/784820/Lys/2'>two lysine residues</scene>; in this structure, they interact with a phosphate.
 </StructureSection>
 == References ==
 <references/>