1dep: Difference between revisions
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==MEMBRANE PROTEIN, NMR, 1 STRUCTURE== | ==MEMBRANE PROTEIN, NMR, 1 STRUCTURE== | ||
<StructureSection load='1dep' size='340' side='right' caption='[[1dep]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1dep' size='340' side='right'caption='[[1dep]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dep]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DEP FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dep]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DEP FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Adrenergic receptor|Adrenergic receptor]] | *[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Jung, H]] | [[Category: Jung, H]] | ||
[[Category: Schnackerz, K D]] | [[Category: Schnackerz, K D]] | ||
Revision as of 03:09, 6 June 2019
MEMBRANE PROTEIN, NMR, 1 STRUCTUREMEMBRANE PROTEIN, NMR, 1 STRUCTURE
Structural highlights
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. Publication Abstract from PubMedThe C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (Gs) [Palm et al. (1989) FEBS Lett. 254, 89-93]. We have investigated the structure of synthetic peptides corresponding to residues 284-295 of the turkey erythrocyte adrenoceptor in micelles, trifluoroethanol and aqueous solution, by using 2D 1H NMR and CD. In the presence of phospholipid micelles the peptides display a C-terminal alpha-helical region, whereas the N-terminal part was found to be highly flexible. NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.,Jung H, Windhaber R, Palm D, Schnackerz KD FEBS Lett. 1995 Jan 23;358(2):133-6. PMID:7828722[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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