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[[Image:Movie Frame 6.png |100 px|left|thumb|Fig. 10: Ballooned pocket functioning as anchoring site for glucagon residues 1-4.]]
[[Image:Movie Frame 6.png |100 px|left|thumb|Fig. 10: Ballooned pocket functioning as anchoring site for glucagon residues 1-4.]]
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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"/>

Revision as of 20:45, 20 April 2016

7TM structure of human class B GPCR 4L6R

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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. 9: Location of anchoring pocket within central cavity.
Fig. 9: Location of anchoring pocket within central cavity.[1]
Fig. 10: Ballooned pocket functioning as anchoring site for glucagon residues 1-4.
Fig. 10: Ballooned pocket functioning as anchoring site for glucagon residues 1-4.
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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