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 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>. | 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 '''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. | 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. | ||
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In the '''FN III''' domains, there are two conserved '''cysteines''' ('''Cys-672 and Cys-751''' <ref>Leptin receptor activation depends on critical cysteine residues in its fibronectin type III subdomains : https://www.jbc.org/article/S0021-9258(20)61429-6/fulltext </ref>) that are crucial for the activation of the receptor. | In the '''FN III''' domains, there are two conserved '''cysteines''' ('''Cys-672 and Cys-751''' <ref>Leptin receptor activation depends on critical cysteine residues in its fibronectin type III subdomains : https://www.jbc.org/article/S0021-9258(20)61429-6/fulltext </ref>) that are crucial for the activation of the receptor. | ||
Moreover, in order to form an '''activated 2:4 leptin:ObR complex''', the leptin clusters '''two pre-formed ObR dimers'''. | |||
== '''Signaling pathways''' == | == '''Signaling pathways''' == | ||
