7-transmembrane receptor

Toll-like receptor - Transmembrane proteins involved in the recognition of components of pathogens that... 

Hebert, T. E., Moffett, S., Morello, J. P., Loisel, T. P., Bichet, D. G., Barret, C., and Bouvier, M. (1996) A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J. Biol. Chem. 271,16384-16392. 

Spier AD, Lummis SC. Immunological characterization of 5-HT3 receptor transmembrane topology. J Mol Neurosci 2002 18(3) 169-178. 

Kim MK, Huang ZY, Hwang PH, et al. Fcgamma receptor transmembrane domains role in cell surface expression, gamma chain interaction, and phagocytosis. Blood 2003 101(ll) 4479-84. 

The modes of action of different alkaloids are diverse. For example, nicotine binds to and affects nicotinic acetylcholine receptors and shows toxicity. A recent molecular 3D model suggests that both acetylcholine and nicotine bind to the same pocket formed in a nicotinic acetylcholine receptor.15 Morphine binds to and activates opioid receptors, transmembrane-spanning G protein-coupled receptors, in the central nervous system of humans.16 Caffeine, which is structurally similar to adenine, inhibits cyclic AMP phosphodiesterase activity and inhibits the degradation of cAMP, thus exerting a toxic effect on insects 17 in human beings, binding of caffeine to the adenosine A2A receptor induces wakefulness.18 Atropine binds to muscarinic acetylcholine receptors, competing with acetylcholine, and blocks neurotransmission.1... 

Proteins are targeted to various locations after synthesis by signal sequences. Thus, proteins destined for the ER, the mitochondria and chloroplasts have particular kinds of signal sequences at the N-terminus. ER-targeted proteins enter the ER directly off rough ER ribosomes via a signal recognition particle (SRP) complex that is linked to an SRP receptor and a ribosome receptor-transmembrane peptide translocation complex associated with the ER membrane. Within, the ER polypeptides are processed and folded and S—S links are formed. 

Fig. 4 A molecular model of the dopamine D2 receptor with a ligand docked in the binding site. The model of the D2 receptor transmembrane helices was constructed from the coordinates of the bacteriorhodopsin structure derived from two-dimensional electron diffraction experiments and is consistent with the projection structure for rhodopsin. The transmembrane helices are represented by a solid ribbon and the drug, apomorphine, is a space filling representation. The top view looking down the helical axis of the receptor clearly delineates the seven transmembrane helices that are the key structural motif for the GPCR superfamily. Some of the helices are inclined relative to the perpendicular to the membrane plane. The bottom view is in the plane of the membrane with the extracellular space at the top of the figure. (Adapted from Ref.t f)...

Anti-asialoglycoprotein receptor Transmembrane antigen bin g AIH, correlate with activity, disappear -... 

All endogenous ligands (small or huge, cationic or not, peptidic or not) can interact with a homologous region of the receptor transmembrane domain. 

Plate 19 A model of BIBP 3226 binding to the hYl-receptor. Transmembrane helices of the hYl-receptor are indicated by a solid ribbon in yellow and labeled in red. Amino-acid side chains of the human Y1 receptor suggested to interact with the antagonist BIBP 3226 (in green) are shown in yellow. 

Signal transduction Intramembrane proteolytic cleavage of receptor transmembrane domain with release of cytosolic segment that functions as co-activator for nuclear... 

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