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Elizeu/sandbox/citocromo c

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Revision as of 18:47, 12 July 2017

Crystal structure of the human beta2 adrenoceptor

Structural highlights

2r4s is a 3 chain structure with sequence from Human and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2r4r
Gene:	ADRB2, ADRB2R, B2AR (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ADRB2_HUMAN] Beta-adrenergic receptors are G Protein-Coupled Receptors, which means that they mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs.

Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.,Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK Nature. 2007 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:17952055^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature. 2007 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:17952055 doi:10.1038/nature06325

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

Julie Langlois, Atena Farhangian, Rebecca Holstein, Elizabeth A. Dunlap, Katherine Reynolds, Elizeu Santos, Noam Gonen, Anna Lohning, Idan Ben-Nachum, Brian Ochoa, Shai Biran, Gauri Misra, Shira Weingarten-Gabbay, Keni Vidilaseris, Jamie Costa, Abhinav Mittal, Urs Leisinger, Madison Walberry, Edmond R Atalla, Brett M. Thumm, Brooke Fenn, Joel L. Sussman, Mati Cohen, Vesta Nwankwo, Dotan Shaniv, Gulalai Shah

Retrieved from "http://52.214.119.220/wiki/index.php/Elizeu/sandbox/citocromo_c"

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 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors are [[G_protein-coupled_receptors]] mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
+[[http://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors are [[G Protein-Coupled Receptors]], which means that they mediate the catecholamine-induced activation of [[adenylate cyclase]] through the action of [[G proteins]]. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

Elizeu/sandbox/citocromo c

From Proteopedia

Revision as of 18:47, 12 July 2017

Crystal structure of the human beta2 adrenoceptor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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