Sandbox Reserved 1473: Difference between revisions
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'''STRUCTURE HIGHLIGHTS''' | '''STRUCTURE HIGHLIGHTS''' | ||
==STRUCTURE HIGHLIGHTS== | |||
<StructureSection load='2rh1' size='450' side='right' caption='Human Beta adrenergic receptor' scene=''> | |||
Structural components of the B2 GPCR. | |||
G-Protein Coupled Receptors (GPCR), also known as 7 transmembrane receptors [because of its 7 constituent alpha helices] are the largest groups of transmembrane protein receptors in eukaryotes. There are many different classes GPCRs depending on their functionality. These include the classes A, B, C, D, E, AND F. Beta adrenergic receptors fall the class C with other metabotropic hormones. All studied GPCRs have a particular structure that can be subdivided into; the amino-terminal extracellular domain, the three extracellular loops (EC1), (EC2), (EC3), the seven spanning transmembrane domains (7TM), three intracellular domains (IC1, ...IC3) and the carboxyl-terminal intracellular domain. The binding of the receptor to a ligand causes a structural change in the intracellular domains that leads to the exchange of GDP for GTP. | |||
</StructureSection> | |||
G-Protein Coupled Receptors (GPCR), also known as 7 transmembrane receptors [because of its 7 constituent alpha helices] are the largest groups of transmembrane protein receptors in eukaryotes. There are many different classes GPCRs depending on their functionality. These include the classes A, B, C, D, E, AND F. Beta adrenergic receptors fall the class C with other metabotropic hormones. All studied GPCRs have a particular structure that can be subdivided into; the amino-terminal extracellular domain, the three extracellular loops (EC1), (EC2), (EC3), the seven spanning transmembrane domains (7TM), three intracellular domains (IC1, ...IC3) and the carboxyl-terminal intracellular domain. The binding of the receptor to a ligand causes a structural change in the intracellular domains that leads to the exchange of GDP for GTP. | G-Protein Coupled Receptors (GPCR), also known as 7 transmembrane receptors [because of its 7 constituent alpha helices] are the largest groups of transmembrane protein receptors in eukaryotes. There are many different classes GPCRs depending on their functionality. These include the classes A, B, C, D, E, AND F. Beta adrenergic receptors fall the class C with other metabotropic hormones. All studied GPCRs have a particular structure that can be subdivided into; the amino-terminal extracellular domain, the three extracellular loops (EC1), (EC2), (EC3), the seven spanning transmembrane domains (7TM), three intracellular domains (IC1, ...IC3) and the carboxyl-terminal intracellular domain. The binding of the receptor to a ligand causes a structural change in the intracellular domains that leads to the exchange of GDP for GTP. | ||
