Sandbox Reserved 1167: Difference between revisions

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==Class B Human Glucagon G-Protein Coupled Receptor==

~~This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~

~~You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~

== Background ==

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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.

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. 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. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of the 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 the GCGR is located deeper inside the molecule.

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

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 ==Class B Human Glucagon G-Protein Coupled Receptor==
 <StructureSection load='4l6r' size='340' side='right' caption='Human Glucagon Class B GPCR ( 7tm PDB: [[4l6r]], ECD PDB: [[4ers]])' scene='72/721538/Glucagon_receptor/1'>
-This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 == Background ==
@@ Line 30: / 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.
+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. 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. As a result, the [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820480/bin/nihms495648f2.jpg binding cavity] of the 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 the GCGR is located deeper inside the molecule.
 ====Other Unique Structural Features ====