Sandbox Reserved 1711 - Revision history

Sophie Mullinix at 19:08, 29 March 2022

Sophie Mullinix — Tue, 29 Mar 2022 19:08:03 GMT

←Older revision		Revision as of 19:08, 29 March 2022
Line 23:		Line 23:
	The <scene name='90/904316/Grd_domains/2'>GRD</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.		The <scene name='90/904316/Grd_domains/2'>GRD</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
-	An <scene name='90/~~905640~~/Arg_finger/1'>~~R1276~~</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.	+	An <scene name='90/904316/Arg_finger/2'>Arginine finger</scene>(R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.
	== Function ==		== Function ==
	The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.		The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.

Sophie Mullinix at 19:00, 29 March 2022

Sophie Mullinix — Tue, 29 Mar 2022 19:00:27 GMT

←Older revision		Revision as of 19:00, 29 March 2022
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	=== Domains ===		=== Domains ===
-	The <scene name='90/904316/Grd_domains/1'>GRD ~~domain~~</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.	+	The <scene name='90/904316/Grd_domains/2'>GRD</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.		An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.

Sophie Mullinix at 18:44, 29 March 2022

Sophie Mullinix — Tue, 29 Mar 2022 18:44:14 GMT

←Older revision		Revision as of 18:44, 29 March 2022
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	=== Domains ===		=== Domains ===
-	The <scene name='90/~~905640~~/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.	+	The <scene name='90/904316/Grd_domains/1'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.		An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.

Sophie Mullinix at 20:12, 28 March 2022

Sophie Mullinix — Mon, 28 Mar 2022 20:12:29 GMT

←Older revision		Revision as of 20:12, 28 March 2022
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	The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.		The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
-	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.	+	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a <scene name='90/904316/Closed_triade/1'>triade</scene> of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.
	== Function ==		== Function ==
	The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.		The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.

Sophie Mullinix at 19:40, 28 March 2022

Sophie Mullinix — Mon, 28 Mar 2022 19:40:08 GMT

←Older revision		Revision as of 19:40, 28 March 2022
Line 23:		Line 23:
	The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.		The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
-	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.	+	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) <scene name='90/904316/Arg_finger/1'>R1276</scene> present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.
	== Function ==		== Function ==
	The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.		The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.

Sophie Mullinix at 19:26, 28 March 2022

Sophie Mullinix — Mon, 28 Mar 2022 19:26:15 GMT

←Older revision		Revision as of 19:26, 28 March 2022
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	=== Conformation: Closed ===		=== Conformation: Closed ===
-	In the overall ~~closed~~ <scene name='90/905640/Closedoverall/1'>closed neurofibromin</scene> and inactive conformation ~~of the neurofibromin protein~~, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive. The closed conformation has both protomers/chains in the closed ~~structure~~, whereas the open conformation has one closed and one open protomer. You can see that in the closed conformation, Ras binding by the GRD domain is sterically hindered and there is no room for association with the Ras protein.	+	In the overall <scene name='90/905640/Closedoverall/1'>closed neurofibromin</scene> (and inactive) conformation, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive. The closed conformation has both of the protomers/chains in the closed positions, whereas the open conformation has one closed and one open protomer. You can see that in the closed conformation, Ras binding by the GRD domain is sterically hindered and there is no room for association with the Ras protein.
	The closed conformation has the GRD and Sec14-PH domains oriented in a way that the amino acids C1032, H1558, and H1576 are in close proximity to each other to form a transition metal-binding site with zinc. The fourth coordination partner in this is water.		The closed conformation has the GRD and Sec14-PH domains oriented in a way that the amino acids C1032, H1558, and H1576 are in close proximity to each other to form a transition metal-binding site with zinc. The fourth coordination partner in this is water.
	<scene name='90/905640/Closedoverall/6'>vertical view</scene>		<scene name='90/905640/Closedoverall/6'>vertical view</scene>
Line 23:		Line 23:
	The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.		The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
-	~~This is because an~~ <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.	+	An <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.
	== Function ==		== Function ==
-		+	The GRD arginine finger (R1276) is crucial in Ras binding. When Neurofibromin is in the open conformation, the Arginine finger is able to bind with Ras because the Arginine is not inhibited as it would be in the closed conformation, where R1276 is facing the core and inaccessible due to the rotation of the two domains. This open conformation allows neurofibromin to associate with Ras via R1276 binding, which then hydrolyzes the Ras from active GTP to inactive GDP, showing why R1276 is crucial to neurofibromin function. In the open conformation, on the other hand, the arginine finger is able to interact with Ras and hydrolyze it which effectively turns it off.
	=== Ras Control ===		=== Ras Control ===
	Ras is still promoting cell proliferation in this closed conformation because Neurofibromin is unable to hydrolyze Ras and inactivate it. In this open conformation, the Ras is not sterically hindered and the Arginine finger is accessible for Ras binding, thus allowing Neurofibromin to down-regulate Ras.		Ras is still promoting cell proliferation in this closed conformation because Neurofibromin is unable to hydrolyze Ras and inactivate it. In this open conformation, the Ras is not sterically hindered and the Arginine finger is accessible for Ras binding, thus allowing Neurofibromin to down-regulate Ras.

Sophie Mullinix at 19:20, 28 March 2022

Sophie Mullinix — Mon, 28 Mar 2022 19:20:46 GMT

←Older revision		Revision as of 19:20, 28 March 2022
Line 23:		Line 23:
	The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.		The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
	=== Key Players ===		=== Key Players ===
-	This is because an <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains.	+	This is because an <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains. The Closed conformation is stabilized by a triade of residues that are coordinated with transition metal-binding sites with zinc. Here, the GRD and Sec14-PH domains are oriented in a way that the H1558 and H1576 are able to interact with C1032 and form a transition binding-site with zinc. This binding site stabilizes the closed conformation and prevents Ras from associating with the GRD based on the location of the GRD in relation to the rest of the protein.
-	Closed conformation is stabilized by ~~one cysteine and two histidines~~ that are coordinated with transition metal-binding sites with zinc.	+
	== Function ==		== Function ==

Sophie Mullinix at 19:10, 28 March 2022

Sophie Mullinix — Mon, 28 Mar 2022 19:10:58 GMT

←Older revision		Revision as of 19:10, 28 March 2022
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-	~~{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->~~	+	= Neurofibromin =
-	==~~Your Heading Here (maybe something like 'Structure')==~~	+
-	~~<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>~~	+
-	~~This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~	+
-	~~You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~	+

		+	<StructureSection load='7pgr' size='340' side='right' caption='Closed conformation of Neurofibromin' scene='90/905640/Closedoverall/1'>
		+
		+	---
		+
		+	[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692384/]
		+
		+	[[Image:Open.jpg\|400px\|right\|thumb\|Figure_1]]
		+
		+	== Introduction ==
		+	<ref name="Bergoug">PMID:33121128</ref>
		+	== Structure ==
		+	Neurofibromin is a <scene name='90/905640/Homodimer/1'>homodimer</scene> with two identical chains (depicted as lime and cyan).
		+	=== Conformation: Open ===
		+
		+	=== Conformation: Closed ===
		+	In the overall closed <scene name='90/905640/Closedoverall/1'>closed neurofibromin</scene> and inactive conformation of the neurofibromin protein, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive. The closed conformation has both protomers/chains in the closed structure, whereas the open conformation has one closed and one open protomer. You can see that in the closed conformation, Ras binding by the GRD domain is sterically hindered and there is no room for association with the Ras protein.
		+	The closed conformation has the GRD and Sec14-PH domains oriented in a way that the amino acids C1032, H1558, and H1576 are in close proximity to each other to form a transition metal-binding site with zinc. The fourth coordination partner in this is water.
		+	<scene name='90/905640/Closedoverall/6'>vertical view</scene>
		+
		+	=== Domains ===
		+	The <scene name='90/905640/Grd_domains/2'>GRD domain</scene> of Neurofibromin, specifically the arginine finger (R1276), binds to the Ras + GTP complex.
		+	=== Key Players ===
		+	This is because an <scene name='90/905640/Arg_finger/1'>R1276</scene> (R1276) present in the GRD is critical for Ras binding and is only accessible when the GRD and Sec14-PH domains are rotated in such a way that there is no steric hindrance from the surrounding dimer chains.
		+	Closed conformation is stabilized by one cysteine and two histidines that are coordinated with transition metal-binding sites with zinc.
	== Function ==		== Function ==

-	== ~~Disease~~ ==	+	=== Ras Control ===
		+	Ras is still promoting cell proliferation in this closed conformation because Neurofibromin is unable to hydrolyze Ras and inactivate it. In this open conformation, the Ras is not sterically hindered and the Arginine finger is accessible for Ras binding, thus allowing Neurofibromin to down-regulate Ras.
		+	=== Mutated ===

-	== ~~Relevance~~ ==	+	== Diseases ==
		+	<ref name="Ransey">PMID:28504306</ref>

-	== Structural highlights ==

-	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>
		+
		+	== Student Contributors ==
		+	*Hannah Luchinski

Jaime Prilusky at 15:30, 14 February 2022

Jaime Prilusky — Mon, 14 Feb 2022 15:30:04 GMT

←Older revision		Revision as of 15:30, 14 February 2022
Line 1:		Line 1:
-	{{~~https://proteopedia.org/w/~~Template:~~Sandbox_Reserved_Eric_Martz_3~~}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->	+	{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
	==Your Heading Here (maybe something like 'Structure')==		==Your Heading Here (maybe something like 'Structure')==
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

OCA: New page: {{https://proteopedia.org/w/Template:Sandbox_Reserved_Eric_Martz_3}} ==Your Heading Here (maybe something like 'Structure')==
OCA — Mon, 14 Feb 2022 15:21:51 GMT

New page: {{https://proteopedia.org/w/Template:Sandbox_Reserved_Eric_Martz_3}} ==Your Heading Here (maybe something like 'Structure')== <StructureSection l...

New page
{{https://proteopedia.org/w/Template:Sandbox_Reserved_Eric_Martz_3}}
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>