Sandbox Reserved 1181

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(New page: {{Sandbox_Reserved_CH462_Central_Metabolism}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' s...)
Current revision (22:08, 20 April 2016) (edit) (undo)
 
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{{Sandbox_Reserved_CH462_Central_Metabolism}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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<Structure load='4L6R' size='350' frame='true' align='right' caption='7TM structure of human class B GPCR 4L6R' scene='72/727091/Full_structure_with_labels/1'/>
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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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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.
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== Function ==
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<scene name='72/727091/Full_Structure_with_Labels/1'>Labels</scene>
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== Disease ==
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<scene name='72/721552/Ligand_binding_interactions/1'>Ligand Binding Interactions and Crucial Disulfide Bond</scene>
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== Relevance ==
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<scene name='72/721552/Glucagon_binding/3'>Glucagon Binding Full Rendering</scene>
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== Structural highlights ==
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<scene name='72/721552/Glucagon_binding_zoomed_in/1'>Glucagon Binding Zoomed in</scene>
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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Old Stuff:
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</StructureSection>
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[[Image:ALA135PRO stalk unwinding.png|150 px|left|thumb|Fig. 1: A135P Mutation and effect on stalk stability <ref name= "Siu 2013"/>. ]] [[Image:Gln142 Tyr138 Glucagon interaction.png|150 px|right|thumb|Fig. 2: Stalk stabilized by salt bridge between Glu133-Lys136. Residues in yellow are demonstrated to have an effect on ligand binding affinity.<ref name= "Siu 2013"/>]]
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== References ==
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<references/>
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[[Image:Asn_298__Trp_295.png|150 px|left|thumb|Fig. 3: Active sites linked to glucagon binding affinity located on ECL1 are labeled<ref name= "Siu 2013"/>.]]
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[[Image:Corticotropin class B and Glucagon class B receptors aligned.png |150 px|left|thumb|Fig. 4: Corticotropin-releasing factor 1 and glucagon receptors; Class B GPCRs with notable central splay]] [[Image:Beta2 class A and Glucagon class B receptors aligned.png |150 px|right|thumb|Fig. 5: Beta 2-adrenergic (class A) and glucagon receptors; showing an absence of central splay in Class A GPCRs.]]
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[[Image:Movie_Frame_2.png|100 px|left|thumb|Fig. 7: Active site buried deep in 7TMD of glucagon receptor.]]
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[[Image:Movie_Frame_7.png|175 px|left|thumb|Fig. 14: Distance measurement of GCGR 7TMD Y138-D362 of 19-20 angstroms and labeled with complimentary glucagon interaction residues.]]
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[[Image:H1___Y10_with_measurement.png|175 px|right|thumb|Fig. 15: Distance measurement of H1-Y10 of 22-24 angstroms and labeled with complimentary GCGR 7TMD residue interactions.]]
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===Future research direction===
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Research for Class A GPCRs is much more extensive than for its secretin, class B counterparts, although class B is proving to be a worthwhile to invest researching. The challenge of class B stabilization, expression, and molecular size , has made class B GPCRs particularly hard to assay. Biochemical research has increased in the class B specifications, because it has been realized that receptors can be modulated by more than the agonist and antagonists present in vivo. Leading research consists of a complex interwoven scheme of equilibria manipulation in multi-receptor conformations. <ref name="Salon 2011"/>

Current revision

7TM structure of human class B GPCR 4L6R

Drag the structure with the mouse to rotate

Old Stuff:

Fig. 1: A135P Mutation and effect on stalk stability .
Fig. 1: A135P Mutation and effect on stalk stability [1].
Fig. 2: Stalk stabilized by salt bridge between Glu133-Lys136. Residues in yellow are demonstrated to have an effect on ligand binding affinity.
Fig. 2: Stalk stabilized by salt bridge between Glu133-Lys136. Residues in yellow are demonstrated to have an effect on ligand binding affinity.[1]
Fig. 3: Active sites linked to glucagon binding affinity located on ECL1 are labeled.
Fig. 3: Active sites linked to glucagon binding affinity located on ECL1 are labeled[1].
Fig. 4: Corticotropin-releasing factor 1 and glucagon receptors; Class B GPCRs with notable central splay
Fig. 4: Corticotropin-releasing factor 1 and glucagon receptors; Class B GPCRs with notable central splay
Fig. 5: Beta 2-adrenergic (class A) and glucagon receptors; showing an absence of central splay in Class A GPCRs.
Fig. 5: Beta 2-adrenergic (class A) and glucagon receptors; showing an absence of central splay in Class A GPCRs.
Fig. 7: Active site buried deep in 7TMD of glucagon receptor.
Fig. 7: Active site buried deep in 7TMD of glucagon receptor.
Fig. 14: Distance measurement of GCGR 7TMD Y138-D362 of 19-20 angstroms and labeled with complimentary glucagon interaction residues.
Fig. 14: Distance measurement of GCGR 7TMD Y138-D362 of 19-20 angstroms and labeled with complimentary glucagon interaction residues.
Fig. 15: Distance measurement of H1-Y10 of 22-24 angstroms and labeled with complimentary GCGR 7TMD residue interactions.
Fig. 15: Distance measurement of H1-Y10 of 22-24 angstroms and labeled with complimentary GCGR 7TMD residue interactions.

Future research direction

Research for Class A GPCRs is much more extensive than for its secretin, class B counterparts, although class B is proving to be a worthwhile to invest researching. The challenge of class B stabilization, expression, and molecular size , has made class B GPCRs particularly hard to assay. Biochemical research has increased in the class B specifications, because it has been realized that receptors can be modulated by more than the agonist and antagonists present in vivo. Leading research consists of a complex interwoven scheme of equilibria manipulation in multi-receptor conformations. [2]

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