Sandbox UC 10 - Revision history

Gonzalo Sepúlveda Hermosilla at 22:00, 19 December 2012

2012-12-19T22:00:12Z

←Older revision		Revision as of 22:00, 19 December 2012
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	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
		+


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	== Escenas ==		== Escenas ==
		+
	<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>		<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>
	{{Template:ColorKey_ConSurf}}		{{Template:ColorKey_ConSurf}}
-		+	<scene name='Sandbox_UC_10/Conservacion_evolutiva2/2'>TextToBeDisplayed</scene>
	<scene name='Sandbox_UC_10/Escena2/1'>TextToBeDisplayed</scene>		<scene name='Sandbox_UC_10/Escena2/1'>TextToBeDisplayed</scene>
	----		----

Gonzalo Sepúlveda Hermosilla at 21:18, 19 December 2012

2012-12-19T21:18:54Z

←Older revision		Revision as of 21:18, 19 December 2012
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	== Escenas ==		== Escenas ==
	<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>		<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>
-
	{{Template:ColorKey_ConSurf}}		{{Template:ColorKey_ConSurf}}

-	<scene name='Sandbox_UC_10/~~Scene2~~/1'>~~Estructuras secundarias~~</scene>	+	<scene name='Sandbox_UC_10/Escena2/1'>TextToBeDisplayed</scene>
	----		----

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	<quiz display=simple>		<quiz display=simple>
-	{la pregunta va aquí \| Type = "[]"}	+	{la pregunta va aquí \|Type="[]"}
	-no.		-no.
	+uno.		+uno.
	-si.		-si.

-	{la pregunta va aquí \| Type = "[]"}	+	{la pregunta va aquí \|Type="[]"}
	-no.		-no.
	-si.		-si.

Gonzalo Sepúlveda Hermosilla at 20:34, 19 December 2012

2012-12-19T20:34:42Z

←Older revision		Revision as of 20:34, 19 December 2012
Line 4:		Line 4:

	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
		+

Gonzalo Sepúlveda Hermosilla at 20:31, 19 December 2012

2012-12-19T20:31:56Z

←Older revision		Revision as of 20:31, 19 December 2012
Line 4:		Line 4:

	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
		+


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	== Referencias ==		== Referencias ==
-
-	Ref1<ref>PMID 1234</ref>
-	Ref2 <ref>PMID 12345</ref>

	<references/>		<references/>
	----		----

Gonzalo Sepúlveda Hermosilla at 20:30, 19 December 2012

2012-12-19T20:30:14Z

←Older revision		Revision as of 20:30, 19 December 2012
Line 4:		Line 4:

	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
		+
		+

	== Escenas ==		== Escenas ==
	<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>		<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>

-	{{Template:~~ColorKey_Amino2CarboxyRainbow~~}}	+	{{Template:ColorKey_ConSurf}}

	<scene name='Sandbox_UC_10/Scene2/1'>Estructuras secundarias</scene>		<scene name='Sandbox_UC_10/Scene2/1'>Estructuras secundarias</scene>

Gonzalo Sepúlveda Hermosilla at 20:25, 19 December 2012

2012-12-19T20:25:48Z

←Older revision		Revision as of 20:25, 19 December 2012
Line 4:		Line 4:

	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
-
-	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]
-
-
-
-
-

	== Escenas ==		== Escenas ==
-	<scene name='~~Sandbox_UC_11~~/~~Escena1~~/3'>~~Rainbow~~</scene>	+	<scene name='Sandbox_UC_10/Conservacion_evolutiva/1'>Zonas conservadas evolutivamente</scene>

	{{Template:ColorKey_Amino2CarboxyRainbow}}		{{Template:ColorKey_Amino2CarboxyRainbow}}

Gonzalo Sepúlveda Hermosilla at 20:20, 19 December 2012

2012-12-19T20:20:54Z

←Older revision		Revision as of 20:20, 19 December 2012
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	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png\|200px\|left\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>		<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png\|200px\|left\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>

-	~~[[Image~~:~~1dxx~~.~~png\|200px\|center\|thumb\|Crystal Structure~~ of ~~Human~~ dystrophin, ~~[[1dxx]]]]~~	+	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
-		+
-	[[Image:imag1gonzalo.jpg\|~~left~~\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]	+

	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]		[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]

-	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>	+

Gonzalo Sepúlveda Hermosilla at 20:19, 19 December 2012

2012-12-19T20:19:49Z

←Older revision		Revision as of 20:19, 19 December 2012
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	== N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN ==		== N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN ==

-	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>	+	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png\|200px\|left\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>

	[[Image:1dxx.png\|200px\|center\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]		[[Image:1dxx.png\|200px\|center\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]

Gonzalo Sepúlveda Hermosilla at 20:19, 19 December 2012

2012-12-19T20:19:08Z

←Older revision		Revision as of 20:19, 19 December 2012
Line 1:		Line 1:
	== N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN ==		== N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN ==

-	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>	+	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>
-	Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.	+

-	[[Image:1dxx.png\|200px\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]	+	[[Image:1dxx.png\|200px\|center\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]

	[[Image:imag1gonzalo.jpg\|left\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]		[[Image:imag1gonzalo.jpg\|left\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
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	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]		[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]

		+	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>


-	<scene name='1xjo/Active_site/3'>active site</scene>

Gonzalo Sepúlveda Hermosilla at 20:15, 19 December 2012

2012-12-19T20:15:57Z

←Older revision		Revision as of 20:15, 19 December 2012
Line 6:		Line 6:
	[[Image:1dxx.png\|200px\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]		[[Image:1dxx.png\|200px\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]

-	[[Image:imag1gonzalo.jpg\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]	+	[[Image:imag1gonzalo.jpg\|left\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]

	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]		[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]

←Older revision		Revision as of 20:20, 19 December 2012
Line 3:		Line 3:
	<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png\|200px\|left\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>		<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png\|200px\|left\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>

-	~~[[Image~~:~~1dxx~~.~~png\|200px\|center\|thumb\|Crystal Structure~~ of ~~Human~~ dystrophin, ~~[[1dxx]]]]~~	+	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg\|right\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]
-		+
-	[[Image:imag1gonzalo.jpg\|~~left~~\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]	+

	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]		[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]

-	CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>	+

←Older revision		Revision as of 20:15, 19 December 2012
Line 6:		Line 6:
	[[Image:1dxx.png\|200px\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]		[[Image:1dxx.png\|200px\|thumb\|Crystal Structure of Human dystrophin, [[1dxx]]]]

-	[[Image:imag1gonzalo.jpg\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]	+	[[Image:imag1gonzalo.jpg\|left\|200px\|thumb\|Comparacion de la degeneracion muscular, [[1dxx]]]]

	[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]		[[Image:MW_Folding_Simulations.gif\|200px\|thumb\|[[1dxx]]]]