2y02: Difference between revisions
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===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== | ||
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==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
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
