Sandbox Reserved 1648: Difference between revisions

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The activation of the leptin receptor <ref name="ref3"/> is done through the '''CRH2, IGD and FN III''' domains <ref> The Leptin Receptor Complex: Heavier Than Expected? : https://www.frontiersin.org/articles/10.3389/fendo.2017.00030/full </ref>.

The '''CRH2''' domain is the main leptin binding site on the receptor. This domain is required for the activation of the receptor. It is composed of a region of four consecutive hydrophobic residues. In particular, <scene name='86/868181/Leu_13/1'>Leu13</scene> and '''Leu86~~'''~~ of leptin interact with '''<scene name='86/868181/Leu_504/1'>Leu504</scene>''' (pink in viewer) in CRH2 forming a bond via hydrophobic interactions<ref>Mapping of the interface between leptin and the leptin receptor CRH2 domain : https://jcs.biologists.org/content/118/11/2519 </ref>. In contrast, the receptor functionality is hardly affected when the CRH1 domain is deleted.

The '''CRH2''' domain is the main leptin binding site on the receptor. This domain is required for the activation of the receptor. It is composed of a region of four consecutive hydrophobic residues. In particular, <scene name='86/868181/Leu_13/1'>Leu13</scene> and <scene name='86/868181/Leu_86/1'>Leu86</scene> of leptin interact with '''<scene name='86/868181/Leu_504/1'>Leu504</scene>''' (pink in viewer) in CRH2 forming a bond via hydrophobic interactions<ref>Mapping of the interface between leptin and the leptin receptor CRH2 domain : https://jcs.biologists.org/content/118/11/2519 </ref>. In contrast, the receptor functionality is hardly affected when the CRH1 domain is deleted.

The '''IGD''' domain has no affinity for leptin but is nevertheless '''required''' for receptor activation. In the absence of this domain, the result is a receptor with a wild-type affinity for leptin. However, the receptor is completely devoid of biological activity.

Sandbox Reserved 1648: Difference between revisions

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 The activation of the leptin receptor <ref name="ref3"/> is done through the '''CRH2, IGD and FN III''' domains <ref> The Leptin Receptor Complex: Heavier Than Expected? : https://www.frontiersin.org/articles/10.3389/fendo.2017.00030/full </ref>.
-The '''CRH2''' domain is the main leptin binding site on the receptor. This domain is required for the activation of the receptor. It is composed of a region of four consecutive hydrophobic residues. In particular, <scene name='86/868181/Leu_13/1'>Leu13</scene> and '''Leu86''' of leptin interact with '''<scene name='86/868181/Leu_504/1'>Leu504</scene>''' (pink in viewer) in CRH2 forming a bond via hydrophobic interactions<ref>Mapping of the interface between leptin and the leptin receptor CRH2 domain : https://jcs.biologists.org/content/118/11/2519 </ref>. In contrast, the receptor functionality is hardly affected when the CRH1 domain is deleted.
+The '''CRH2''' domain is the main leptin binding site on the receptor. This domain is required for the activation of the receptor. It is composed of a region of four consecutive hydrophobic residues. In particular, <scene name='86/868181/Leu_13/1'>Leu13</scene> and <scene name='86/868181/Leu_86/1'>Leu86</scene> of leptin interact with '''<scene name='86/868181/Leu_504/1'>Leu504</scene>''' (pink in viewer) in CRH2 forming a bond via hydrophobic interactions<ref>Mapping of the interface between leptin and the leptin receptor CRH2 domain : https://jcs.biologists.org/content/118/11/2519 </ref>. In contrast, the receptor functionality is hardly affected when the CRH1 domain is deleted.
 The '''IGD''' domain has no affinity for leptin but is nevertheless '''required''' for receptor activation. In the absence of this domain, the result is a receptor with a wild-type affinity for leptin. However, the receptor is completely devoid of biological activity.