Adrenergic receptor

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===β-2 adrenergic receptor===
===β-2 adrenergic receptor===
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<table width=309' align='right' cellpadding='0'><tr><td rowspan='2'>&nbsp;</td><td bgcolor='#eeeeee'>[[Image:7tm labeled.png|right|300px]]</td></tr><tr><td bgcolor='#eeeeee'><center>
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β2 adrenergic receptor binding a hormone analog<br/> and complexed to a heterotrimeric G protein ([[3sn6]])
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</center></td></tr></table>
{{Template:GPCR3sn6}}
{{Template:GPCR3sn6}}
See also [[Beta-2 Adrenergic Receptor]]<br />
See also [[Beta-2 Adrenergic Receptor]]<br />

Revision as of 04:17, 8 December 2012

Crystal Structure of β-2 Adrenergic Receptor, 2rh1
Crystal Structure of β-2 Adrenergic Receptor, 2rh1

PDB ID 2rh1

Drag the structure with the mouse to rotate
β-2 Adrenergic Receptor, 2rh1
Ligands: , , , , , , ,
Gene: ADRB2, ADRB2R, B2AR / E (Enterobacteria phage T4)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



The adrenergic receptors are metabolic G protein-coupled receptors. They are the targets of catecholamines. The binding of an agonist to them causes a sympathetic response. The α-2 adrenergic receptor (A2AR) inhibits insulin or glucagons release. The β-1 adrenergic receptor (B1AR) increases cardiac output and secretion of rennin and ghrelin. The β-2 adrenergic receptor (B2AR) triggers many relaxation reactions. The images at the left and at the right correspond to one representative Adrenergic receptor, i.e. the crystal structure of human β-2 adrenergic Receptor (2rh1). See also Beta-2 Adrenergic Receptor and G protein-coupled receptor. (morph was taken from Gallery of Morphs of the Yale Morph Server).


Contents

3D Structures of Adrenergic receptor

Update November 2011

α-2 adrenergic receptor

3kj6, 2r4r, 2r4s – hA2AR + FAB heavy+light chains
1ho9, 1hod – hA2AR peptide (mutant) – NMR
1hof, 1hll - hA2AR peptide – NMR

β-1 adrenergic receptor

2y01 – tB1AR fragment (mutant) – turkey
1dep – tB1AR peptide - NMR
2y00, 2y02, 2y03, 2y04, 2vt4 - tB1AR fragment (mutant) + agonist
2ycw, 2ycx, 2ycz, 2ycy - tB1AR fragment (mutant) + antagonist

β-2 adrenergic receptor

 

β2 adrenergic receptor binding a hormone analog
and complexed to a heterotrimeric G protein (3sn6)

 

Drag the structure with the mouse to rotate
An activated G protein-coupled receptor (human β-2 adrenergic receptor in blue ) in a complex with a heterotrimeric G protein (3 subunits:reddish to orange-brown) and hormone (gold) (3sn6), resolution 3.2Å. The boundaries of the membrane in which the GPCR sits are represented in light green.


See also Beta-2 Adrenergic Receptor
3pds - hB2AR/T4 lysozyme - human
3p0g – hB2AR/T4 lysozyme + cameloid antibody fragment
2r4s,2r4r - hB2AR + Fab5 complex
2rh1 - hB2AR/T4 lysozyme (mutant)
3d4s - hB2AR/T4 lysozyme (mutant) + cholesterol
3ny8, 3ny9, 3nya – hB2AR + agonist
3sn6 - human β-2 adrenergic receptor + cameloid antibody fragment bound by guanine nucleotide-binding protein G. This is the first structure of an activated GPCR in a complex with its G protein.
See also The Madison West High School 2008 SMART Team's Page on the β-2 adrenergic receptor

Nobel Prize Related to the Structures

Robert J. Lefkowitz and Brian K. Kobilka share the 2012 Nobel Prize in Chemistry for work on GPCRs that includes solving the first structures of a ligand-activated GPCR (2r4r, 2r4s, & 2rh1 in 2007)[1][2][3] and the first activated GPCR in complex with its G protein (3sn6 in 2011)[4][5][6][7]. A detailed description of the laureates' body of work on this class of receptors with images is here.

References and Notes


See Also

External Resources

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Wayne Decatur, Karsten Theis, Alexander Berchansky

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