Sandbox Reserved 1167: Difference between revisions

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==== Helix I Stalk Region ====

The tip of Helix I extends above the cell membrane into the extracellular space creating a <scene name='72/721538/Helix_i/14'> stalk region</scene>. This region is longer than any other class of GPCR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm<ref ~~name='structure'~~>PMID:23863937/ref>.

The tip of Helix I extends above the cell membrane into the extracellular space creating a <scene name='72/721538/Helix_i/14'> stalk region</scene>. This region is longer than any other class of GPCR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm<ref>PMID:23863937</ref>.

==== Intracellular Helix VIII ====

The GCGR also contains an intracellular Helix VIII that is comprised of roughly 20 amino acids at the C-terminal end. This helix tilts approximately 25 degrees away from the membrane - the corresponding position in class A receptors are turned toward the membrane<ref ~~name="1"~~/>. Although researchers are not entirely sure of its function, this helix is completely conserved in class B structures.

The GCGR also contains an intracellular Helix VIII that is comprised of roughly 20 amino acids at the C-terminal end. This helix tilts approximately 25 degrees away from the membrane - the corresponding position in class A receptors are turned toward the membrane<ref>PMID:23863937</ref>. Although researchers are not entirely sure of its function, this helix is completely conserved in class B structures.

==== Binding Pocket ====

The class B GPCR has the widest and longest binding pocket. The distance between the EC tips of Helicies II and VI as well as between the tips of Helicies III and VII are some of the largest among the GPCRs<ref ~~name="1"~~/>. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of GCGR is located deeper inside the molecule.

The class B GPCR has the widest and longest binding pocket. The distance between the EC tips of Helicies II and VI as well as between the tips of Helicies III and VII are some of the largest among the GPCRs<ref>PMID:23863937</ref>. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of GCGR is located deeper inside the molecule.

====Other Unique Structural Features ====

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@@ Line 27: / Line 27: @@
 ==== Helix I Stalk Region ====
-The tip of Helix I extends above the cell membrane into the extracellular space creating a <scene name='72/721538/Helix_i/14'> stalk region</scene>. This region is longer than any other class of GPCR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm<ref name='structure'>PMID:23863937/ref>.
+The tip of Helix I extends above the cell membrane into the extracellular space creating a <scene name='72/721538/Helix_i/14'> stalk region</scene>. This region is longer than any other class of GPCR and extends 3 α-helical turns above the plane of the membrane. It helps to capture the glucagon peptide and facilitates it's insertion into the 7tm<ref>PMID:23863937</ref>.
 ==== Intracellular Helix VIII ====
-The GCGR also contains an intracellular Helix VIII that is comprised of roughly 20 amino acids at the C-terminal end. This helix tilts approximately 25 degrees away from the membrane - the corresponding position in class A receptors are turned toward the membrane<ref name="1"/>. Although researchers are not entirely sure of its function, this helix is completely conserved in class B structures.
+The GCGR also contains an intracellular Helix VIII that is comprised of roughly 20 amino acids at the C-terminal end. This helix tilts approximately 25 degrees away from the membrane - the corresponding position in class A receptors are turned toward the membrane<ref>PMID:23863937</ref>. Although researchers are not entirely sure of its function, this helix is completely conserved in class B structures.
 ==== Binding Pocket ====
-The class B GPCR has the widest and longest binding pocket. The distance between the EC tips of Helicies II and VI  as well as between the tips of Helicies III and VII are some of the largest among the GPCRs<ref name="1"/>. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of GCGR is located deeper inside the molecule.
+The class B GPCR has the widest and longest binding pocket. The distance between the EC tips of Helicies II and VI  as well as between the tips of Helicies III and VII are some of the largest among the GPCRs<ref>PMID:23863937</ref>. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of GCGR is located deeper inside the molecule.
 ====Other Unique Structural Features ====