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''')

- an immunoglobuline-like domain ('''IGD ''' (<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>)) <ref> https://www.ncbi.nlm.nih.gov/Structure/icn3d/full.html?&mmdbid=97998&bu=1&showanno=1&source=full-feature </ref> <ref name="ref4"> </ref>

- an immunoglobuline-like domain ('''IGD ''' (<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>)) <ref name="refe"> https://www.ncbi.nlm.nih.gov/Structure/icn3d/full.html?&mmdbid=97998&bu=1&showanno=1&source=full-feature </ref> <ref name="ref4"> </ref>

- two additional membrane-proximal fibronectin type III ('''FN 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 ('''FN 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> <ref name="refe"> </ref>.

ObR is heavily glycosylated causing an increase of 30-70 kDa in molecular weight <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 '''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.

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 <ref name="refe"> </ref> .

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 <ref name="refe"> </ref>.

Moreover, in order to form an '''<scene name='86/868181/Activated_leptin_obr_complex/1'>activated 2:4 leptin:ObR complex</scene>'''., the leptin clusters '''two pre-formed ObR dimers'''.

Sandbox Reserved 1648: Difference between revisions

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@@ Line 20: / Line 20: @@
 - 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 ''' (<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>)) <ref> https://www.ncbi.nlm.nih.gov/Structure/icn3d/full.html?&mmdbid=97998&bu=1&showanno=1&source=full-feature </ref> <ref name="ref4"> </ref>
+- an immunoglobuline-like domain ('''IGD ''' (<scene name='86/868181/Igd/1'>IGD heavy chain</scene> and <scene name='86/868181/Igd/2'>IGD light chain</scene>)) <ref name="refe"> https://www.ncbi.nlm.nih.gov/Structure/icn3d/full.html?&mmdbid=97998&bu=1&showanno=1&source=full-feature </ref> <ref name="ref4"> </ref>
-- two additional membrane-proximal fibronectin type III ('''FN 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 ('''FN 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> <ref name="refe"> </ref>.
 ObR is heavily glycosylated causing an increase of 30-70 kDa in molecular weight <ref name="refl"> </ref> .
@@ Line 58: / Line 58: @@
 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''' (<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.
+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 <ref name="refe"> </ref> .
-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 <ref name="refe"> </ref>.
 Moreover, in order to form an '''<scene name='86/868181/Activated_leptin_obr_complex/1'>activated 2:4 leptin:ObR complex</scene>'''., the leptin clusters '''two pre-formed ObR dimers'''.