Sandbox Reserved 1648: Difference between revisions
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- two CRH domains (a distal membrane homology of the first cytokine receptor '''CHR1''' and a second homology of the cytokine receptor '''CRH2''') | - two CRH domains (a distal membrane homology of the first cytokine receptor '''CHR1''' and a second homology of the cytokine receptor '''CRH2''') | ||
- an immunoglobuline-like domain ('''IGD''') | - an immunoglobuline-like domain ('''<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>''') | ||
- two additional membrane-proximal fibronectin type III ('''<scene name='86/868181/Fn_iii/1'>single FN III domain</scene> or <scene name='86/868181/Fn_iii/2'>Fn III domains</scene>''') domains <ref> DOI:https://doi.org/10.1016/j.str.2012.01.019 </ref> <ref name="refl"> </ref>. | - two additional membrane-proximal fibronectin type III ('''<scene name='86/868181/Fn_iii/1'>single FN III domain</scene> or <scene name='86/868181/Fn_iii/2'>Fn III domains</scene>''') domains <ref> DOI:https://doi.org/10.1016/j.str.2012.01.019 </ref> <ref name="refl"> </ref>. | ||
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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_504/2'>Leu504</scene>''' 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_504/2'>Leu504</scene>''' 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'''(<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>) 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. | ||
In the '''<scene name='86/868181/Fn_iii/1'>FN III</scene>''' 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 '''<scene name='86/868181/Fn_iii/1'>FN III</scene>''' 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. | ||
