Sandbox WWC9 - Revision history

Dana Emmert at 17:20, 13 May 2016

Dana Emmert — Fri, 13 May 2016 17:20:48 GMT

←Older revision		Revision as of 17:20, 13 May 2016
Line 15:		Line 15:
	=== Architecture ===		=== Architecture ===
	The µ-OR crystalized is that of the Mus musculus and has been given the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA). The crystal structure of the protein shows the seven transmembrane helices characteristic of GPCRs that are connected by three extracellular loops and three intracellular loops. The receptors are arranges in dimers closely associated with transmembrane (TM) helices 5 and 6 (See image). The receptor also displays alternating aqueous and lipidic layers corresponding to transmembrane domains. (2)		The µ-OR crystalized is that of the Mus musculus and has been given the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA). The crystal structure of the protein shows the seven transmembrane helices characteristic of GPCRs that are connected by three extracellular loops and three intracellular loops. The receptors are arranges in dimers closely associated with transmembrane (TM) helices 5 and 6 (See image). The receptor also displays alternating aqueous and lipidic layers corresponding to transmembrane domains. (2)
-	Binding site:	+	=== Binding site ===
	The µ-OR, unlike most GPCRs that possess a buried binding site, contains an open solvent filled binding site of approximately 2173 Å3 and an accessible pocket area of 237Å2. (2,3)		The µ-OR, unlike most GPCRs that possess a buried binding site, contains an open solvent filled binding site of approximately 2173 Å3 and an accessible pocket area of 237Å2. (2,3)
		+
		+	== Function ==
		+
		+
		+	== Ligand Subtypes ==

Dana Emmert at 17:18, 13 May 2016

Dana Emmert — Fri, 13 May 2016 17:18:33 GMT

←Older revision		Revision as of 17:18, 13 May 2016
Line 1:		Line 1:
	== The µ-opioid Receptor (4DKL) ==		== The µ-opioid Receptor (4DKL) ==

-	~~== Introduction ==~~	+
	Opioids are highly specific endogenous and exogenous ligands in function as a means of analgesia and bind to a family of receptor proteins known as the opioid receptors (ORs). The three types of opioid receptors (µ-, κ-, δ-, respectively) belong to the protein superfamily G-protein coupled receptors (GCPRs); transmembrane proteins consisting of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR, exists primarily in the brain, spinal cord, and in the periphery. (1)		Opioids are highly specific endogenous and exogenous ligands in function as a means of analgesia and bind to a family of receptor proteins known as the opioid receptors (ORs). The three types of opioid receptors (µ-, κ-, δ-, respectively) belong to the protein superfamily G-protein coupled receptors (GCPRs); transmembrane proteins consisting of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR, exists primarily in the brain, spinal cord, and in the periphery. (1)

Dana Emmert at 17:12, 13 May 2016

Dana Emmert — Fri, 13 May 2016 17:12:17 GMT

←Older revision		Revision as of 17:12, 13 May 2016
Line 13:		Line 13:

	== Structure ==		== Structure ==
-	Architecture:	+	=== Architecture ===
	The µ-OR crystalized is that of the Mus musculus and has been given the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA). The crystal structure of the protein shows the seven transmembrane helices characteristic of GPCRs that are connected by three extracellular loops and three intracellular loops. The receptors are arranges in dimers closely associated with transmembrane (TM) helices 5 and 6 (See image). The receptor also displays alternating aqueous and lipidic layers corresponding to transmembrane domains. (2)		The µ-OR crystalized is that of the Mus musculus and has been given the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA). The crystal structure of the protein shows the seven transmembrane helices characteristic of GPCRs that are connected by three extracellular loops and three intracellular loops. The receptors are arranges in dimers closely associated with transmembrane (TM) helices 5 and 6 (See image). The receptor also displays alternating aqueous and lipidic layers corresponding to transmembrane domains. (2)
	Binding site:		Binding site:

Dana Emmert at 16:52, 13 May 2016

Dana Emmert — Fri, 13 May 2016 16:52:31 GMT

←Older revision		Revision as of 16:52, 13 May 2016
Line 3:		Line 3:
	== Introduction ==		== Introduction ==
	Opioids are highly specific endogenous and exogenous ligands in function as a means of analgesia and bind to a family of receptor proteins known as the opioid receptors (ORs). The three types of opioid receptors (µ-, κ-, δ-, respectively) belong to the protein superfamily G-protein coupled receptors (GCPRs); transmembrane proteins consisting of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR, exists primarily in the brain, spinal cord, and in the periphery. (1)		Opioids are highly specific endogenous and exogenous ligands in function as a means of analgesia and bind to a family of receptor proteins known as the opioid receptors (ORs). The three types of opioid receptors (µ-, κ-, δ-, respectively) belong to the protein superfamily G-protein coupled receptors (GCPRs); transmembrane proteins consisting of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR, exists primarily in the brain, spinal cord, and in the periphery. (1)
		+
		+	<Structure load='4dkl' size='450' frame='true' align='right' caption='4dkl' scene='Insert optional scene name here' />
		+	<scene name='72/727893/C_to_n_rainbow/1'>See N to C sequence</scene>
		+	{{Template:ColorKey_Amino2CarboxyRainbow}}
		+
		+	Here we can see a <scene name='72/727893/Hydrophobicity/1'>hydrophobicity display</scene> for this protein. Hydrophobic portions of the protein appear in grey, whereas polar potions appear in pink.
		+	{{Template:ColorKey_Hydrophobic}}{{Template:ColorKey_Polar}}
		+

	== Structure ==		== Structure ==
Line 18:		Line 26:

	4. Al-Hasani, R.; Bruchas, M. R. Molecular Mechanisms Of Opioid Receptor-Dependent Signaling and Behavior. Anesthesiology . 2011, 115, 1363–1381.		4. Al-Hasani, R.; Bruchas, M. R. Molecular Mechanisms Of Opioid Receptor-Dependent Signaling and Behavior. Anesthesiology . 2011, 115, 1363–1381.
-
-
-
-	<Structure load='4dkl' size='450' frame='true' align='right' caption='4dkl' scene='Insert optional scene name here' />
-	<scene name='72/727893/C_to_n_rainbow/1'>See N to C sequence</scene>
-	{{Template:ColorKey_Amino2CarboxyRainbow}}
-
-	Here we can see a <scene name='72/727893/Hydrophobicity/1'>hydrophobicity display</scene> for this protein. Hydrophobic portions of the protein appear in grey, whereas polar potions appear in pink.
-	{{Template:ColorKey_Hydrophobic}}{{Template:ColorKey_Polar}}

Dana Emmert at 17:47, 6 May 2016

Dana Emmert — Fri, 06 May 2016 17:47:13 GMT

←Older revision		Revision as of 17:47, 6 May 2016
Line 1:		Line 1:
	== The µ-opioid Receptor (4DKL) ==		== The µ-opioid Receptor (4DKL) ==

		+	== Introduction ==
		+	Opioids are highly specific endogenous and exogenous ligands in function as a means of analgesia and bind to a family of receptor proteins known as the opioid receptors (ORs). The three types of opioid receptors (µ-, κ-, δ-, respectively) belong to the protein superfamily G-protein coupled receptors (GCPRs); transmembrane proteins consisting of 7 membrane-spanning alpha-helical structures in which the extracellular ligand binding pocket exists. The µ-OR, exists primarily in the brain, spinal cord, and in the periphery. (1)

		+	== Structure ==
		+	Architecture:
		+	The µ-OR crystalized is that of the Mus musculus and has been given the protein database (PDB) identification 4DKL. This protein was crystalized on a 2.8 Å resolution with a bound irreversible morphinan antagonist β-funaltrexamine (β-FNA). The crystal structure of the protein shows the seven transmembrane helices characteristic of GPCRs that are connected by three extracellular loops and three intracellular loops. The receptors are arranges in dimers closely associated with transmembrane (TM) helices 5 and 6 (See image). The receptor also displays alternating aqueous and lipidic layers corresponding to transmembrane domains. (2)
		+	Binding site:
		+	The µ-OR, unlike most GPCRs that possess a buried binding site, contains an open solvent filled binding site of approximately 2173 Å3 and an accessible pocket area of 237Å2. (2,3)
		+
		+
		+	== References ==
		+	1. Julian, R., Advokat, C., & Comaty, J. (2011). A Primer of Drug Action (Twelfth Edition). Worth Publishers.
		+	2. Manglic, A.; Kruse , A. C.; Kobilka, T. S.; Thian, F. S.; Mathiesen, J. M.; Sunahara, R. K.; Pardo, L.; Weis, W. I.; Kobilka, B. K.; Granier, S. Crystal Structure Of the µ-Opioid Receptor Bound to a Morphinan Antagonist. Nature. 2012, 485, 321–326.
		+
		+	3. Cui, X.; Yeliseev, A.; Liu, R. Ligand Interaction, Binding Site And G Protein Activation of the Mu Opioid Receptor. Eur J Pharmacol. 2013, 702, 309–315.
		+
		+	4. Al-Hasani, R.; Bruchas, M. R. Molecular Mechanisms Of Opioid Receptor-Dependent Signaling and Behavior. Anesthesiology . 2011, 115, 1363–1381.

Dana Emmert at 17:45, 6 May 2016

Dana Emmert — Fri, 06 May 2016 17:45:39 GMT

←Older revision		Revision as of 17:45, 6 May 2016
Line 2:		Line 2:


-	~~[[Image:MW_Folding_Simulations.gif]]~~	+

Dana Emmert at 20:14, 29 April 2016

Dana Emmert — Fri, 29 Apr 2016 20:14:35 GMT

←Older revision		Revision as of 20:14, 29 April 2016
Line 1:		Line 1:
-
	== The µ-opioid Receptor (4DKL) ==		== The µ-opioid Receptor (4DKL) ==

Line 12:		Line 11:
	Here we can see a <scene name='72/727893/Hydrophobicity/1'>hydrophobicity display</scene> for this protein. Hydrophobic portions of the protein appear in grey, whereas polar potions appear in pink.		Here we can see a <scene name='72/727893/Hydrophobicity/1'>hydrophobicity display</scene> for this protein. Hydrophobic portions of the protein appear in grey, whereas polar potions appear in pink.
	{{Template:ColorKey_Hydrophobic}}{{Template:ColorKey_Polar}}		{{Template:ColorKey_Hydrophobic}}{{Template:ColorKey_Polar}}
-
-
-
-	<quiz display=simple>
-	{How many alpha helices are in this structure?
-	\|type="[]"}
-	-None
-	+One
-	-Four
-	</quiz>
-	[[Link title]]

Dana Emmert at 21:26, 15 April 2016

Dana Emmert — Fri, 15 Apr 2016 21:26:16 GMT

←Older revision		Revision as of 21:26, 15 April 2016
Line 1:		Line 1:
-	<The µ-opioid Receptor (4DKL)	+
		+	== The µ-opioid Receptor (4DKL) ==

Dana Emmert at 21:22, 15 April 2016

Dana Emmert — Fri, 15 Apr 2016 21:22:01 GMT

←Older revision		Revision as of 21:22, 15 April 2016
Line 1:		Line 1:
-	<~~Structure load='~~The µ-opioid Receptor (4DKL)	+	<The µ-opioid Receptor (4DKL)

Dana Emmert at 21:21, 15 April 2016

Dana Emmert — Fri, 15 Apr 2016 21:21:22 GMT

←Older revision		Revision as of 21:21, 15 April 2016
Line 1:		Line 1:
-	'~~'HELLO WORLD!'' WELCOME TO MY '''PROTEOPEDIA''' PAGE, ENJOY!~~	+	<Structure load='The µ-opioid Receptor (4DKL)


Line 5:		Line 5:


-	<Structure load='4dkl' size='~~850~~' frame='true' align='right' caption='~~1pgb~~' scene='Insert optional scene name here' />	+	<Structure load='4dkl' size='450' frame='true' align='right' caption='4dkl' scene='Insert optional scene name here' />
	<scene name='72/727893/C_to_n_rainbow/1'>See N to C sequence</scene>		<scene name='72/727893/C_to_n_rainbow/1'>See N to C sequence</scene>
	{{Template:ColorKey_Amino2CarboxyRainbow}}		{{Template:ColorKey_Amino2CarboxyRainbow}}
Line 21:		Line 21:
	-Four		-Four
	</quiz>		</quiz>
		+	[[Link title]]