Sandbox Reserved 1167: Difference between revisions

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In contrast to class A glucagon receptors which have a [https://en.wikipedia.org/wiki/Proline proline] kink, in all  [https://en.wikipedia.org/wiki/Secretin_receptor_family secretin-like class B glucagon receptors] there is a [https://en.wikipedia.org/wiki/Glycine Glycine] at position 393 in Helix VII which allows for a <scene name='72/721537/Gly_393_helical_bend/1'>helical bend</scene>. This glycine helical bend is fully [https://en.wikipedia.org/wiki/Conserved_sequence conserved] in all secretin-like class B receptors and is an important part of the FQGxxVxxYCF [https://en.wikipedia.org/wiki/Sequence_motif motif].
In contrast to class A glucagon receptors which have a [https://en.wikipedia.org/wiki/Proline proline] kink, in all  [https://en.wikipedia.org/wiki/Secretin_receptor_family secretin-like class B glucagon receptors] there is a [https://en.wikipedia.org/wiki/Glycine Glycine] at position 393 in Helix VII which allows for a <scene name='72/721537/Gly_393_helical_bend/1'>helical bend</scene>. This glycine helical bend is fully [https://en.wikipedia.org/wiki/Conserved_sequence conserved] in all secretin-like class B receptors and is an important part of the FQGxxVxxYCF [https://en.wikipedia.org/wiki/Sequence_motif motif].


Another important structural component found in all secretin-like class B receptors are the two conserved [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] found between [https://en.wikipedia.org/wiki/Arginine Arg] 346 and [https://en.wikipedia.org/wiki/Glutamic_acid Glu] 406 and Arg 173 and Glu 406 [[Image:Salt Bridge Interactions.png | 250 px|right|thumb|Glu 406 Salt Bridges]]. These salt bridges appear to be distinct feature of class B receptors only, however, because there is no conservation of these residues seen in class A receptors.  
Another important structural component found in all secretin-like class B receptors are the two conserved [https://en.wikipedia.org/wiki/Salt_bridge_%28protein_and_supramolecular%29 salt bridges] found between [https://en.wikipedia.org/wiki/Arginine Arg] 346 and [https://en.wikipedia.org/wiki/Glutamic_acid Glu] 406 and Arg 173 and Glu 406 [[Image:Salt Bridge Interactions.png | 250 px|right|thumb|Glu 406 Salt Bridges]]. These salt bridges are a distinct feature of class B receptors only because their interaction results in the distinct stalk found only in class B receptors<ref name ='structure_article'>PMID:23863937</ref>.


A conserved [https://en.wikipedia.org/wiki/Disulfide disulfide bond] can be found in 7tm region at <scene name='72/721538/7tm_disulfide_bond/2'>Cys224-Cys294</scene> which helps to stabilize the 7tm fold. This bond is conserved among both class A and class B receptors. Additionally, the ECD region of Class B GCPRs is defined by three conserved disulfide bonds. These bonds occur at <scene name='72/721538/Ecd_disulfide_bond_1/4'>Cys62-Cys104</scene>, <scene name='72/721538/Ecd_disulfide_bond_2/1'>Cys46-Cys71</scene>, and <scene name='72/721538/Ecd_disulfide_bond_3/1'>Cys85-Cys126</scene>.
A conserved [https://en.wikipedia.org/wiki/Disulfide disulfide bond] can be found in 7tm region at <scene name='72/721538/7tm_disulfide_bond/2'>Cys224-Cys294</scene> which helps to stabilize the 7tm fold. This bond is conserved among both class A and class B receptors. Additionally, the ECD region of Class B GCPRs is defined by three conserved disulfide bonds. These bonds occur at <scene name='72/721538/Ecd_disulfide_bond_1/4'>Cys62-Cys104</scene>, <scene name='72/721538/Ecd_disulfide_bond_2/1'>Cys46-Cys71</scene>, and <scene name='72/721538/Ecd_disulfide_bond_3/1'>Cys85-Cys126</scene>.
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