2y02
From Proteopedia
(Difference between revisions)
Line 2: | Line 2: | ||
===TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL=== | ===TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL=== | ||
{{ABSTRACT_PUBMED_21228877}} | {{ABSTRACT_PUBMED_21228877}} | ||
+ | |||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. | ||
==About this Structure== | ==About this Structure== | ||
Line 11: | Line 14: | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:021228877</ref>< | + | <ref group="xtra">PMID:021228877</ref><references group="xtra"/><references/> |
[[Category: Meleagris gallopavo]] | [[Category: Meleagris gallopavo]] | ||
[[Category: Baker, J G.]] | [[Category: Baker, J G.]] |
Revision as of 06:34, 29 September 2013
Contents |
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL
Template:ABSTRACT PUBMED 21228877
Function
[ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
About this Structure
2y02 is a 2 chain structure with sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
See Also
Reference
- Warne T, Moukhametzianov R, Baker JG, Nehme R, Edwards PC, Leslie AG, Schertler GF, Tate CG. The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor. Nature. 2011 Jan 13;469(7329):241-4. PMID:21228877 doi:10.1038/nature09746