Sandbox Reserved 1167: Difference between revisions

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As opposed 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 | ~~300~~ px|~~left~~|thumb|Glu 406 Salt Bridges]]. No conservation of these residues are 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]]. No conservation of these residues are seen in Class A receptors.

The 7tm region has a conserved [https://en.wikipedia.org/wiki/Disulfide disulfide bond] 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.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>.

As a part of the interface stabilization between helices VI, V, and III, a Class B specific [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bond] occurs between [https://en.wikipedia.org/wiki/Asparagine N] 318 of Helix V and [https://en.wikipedia.org/wiki/Leucine L] 242 of Helix III.

As a part of the interface stabilization between helices VI, V, and III, a Class B-specific [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bond] occurs between [https://en.wikipedia.org/wiki/Asparagine N] 318 of Helix V and [https://en.wikipedia.org/wiki/Leucine L] 242 of Helix III. [[Image:Conserved Class B Residues.png | 250 px|left|thumb|Helical Interactions VI-V-III]]

=== GCGR-Specific Traits ===

Sandbox Reserved 1167: Difference between revisions

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@@ Line 18: / Line 18: @@
 As opposed 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 | 300 px|left|thumb|Glu 406 Salt Bridges]]. No conservation of these residues are 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]]. No conservation of these residues are seen in Class A receptors.
 The 7tm region has a conserved [https://en.wikipedia.org/wiki/Disulfide disulfide bond] 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.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>.
-As a part of the interface stabilization between helices VI, V, and III, a Class B specific [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bond] occurs between [https://en.wikipedia.org/wiki/Asparagine N] 318 of Helix V and [https://en.wikipedia.org/wiki/Leucine L] 242 of Helix III.
+As a part of the interface stabilization between helices VI, V, and III, a Class B-specific [https://en.wikipedia.org/wiki/Hydrogen_bond hydrogen bond] occurs between [https://en.wikipedia.org/wiki/Asparagine N] 318 of Helix V and [https://en.wikipedia.org/wiki/Leucine L] 242 of Helix III. [[Image:Conserved Class B Residues.png | 250 px|left|thumb|Helical Interactions VI-V-III]]
 === GCGR-Specific Traits ===