User:Abla Tannous/Sandbox 1 - Revision history

Abla Tannous at 03:49, 7 January 2013

Abla Tannous — Mon, 07 Jan 2013 03:49:52 GMT

←Older revision		Revision as of 03:49, 7 January 2013
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	== Alpha-1-antitrypsin ==		== Alpha-1-antitrypsin ==
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-	<Structure load='2qug' size='500' frame='true' align='right' caption='Insert caption here'
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-	<scene name='User:Abla_Tannous/Sandbox_1/Glycans_and_rcl/1'>TextToBeDisplayed</scene>
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-	1- Bradley R. Pearse,Taku Tamura,Johan C. Sunryd,Gregory A. Grabowski, Randal J. Kaufman and Daniel N. Hebert. The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin. Journal of Cell Biology. 189; 829-841 (2010)
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-	2- Victoria E. Ahn, Paul Leyko, Jean-René Alattia, Lu Chen, and Gilbert G. Privé. Crystal structures of saposin A and C. Protein Science 15;1849-1857 (2006)

Abla Tannous at 03:30, 7 January 2013

Abla Tannous — Mon, 07 Jan 2013 03:30:20 GMT

←Older revision		Revision as of 03:30, 7 January 2013
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-	== ~~Saposin C domain of prosaposin~~ ==	+	== Alpha-1-antitrypsin ==



-	<Structure load='~~2GTG~~' size='500' frame='true' align='right' caption='Insert caption here' ~~scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1~~	+	<Structure load='2qug' size='500' frame='true' align='right' caption='Insert caption here'

		+	<scene name='User:Abla_Tannous/Sandbox_1/Glycans_and_rcl/1'>TextToBeDisplayed</scene>


-	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>
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-	Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal enzymes (1). Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins(1). Deficiency of UGT1 causes defects in prosaposin maturation(1). Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins(2). The saposin motif is characterized by six cysteines that form three intramolecular disulfide bonds(2). In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic α-helices, where the third helix shows a highly localized kink (2).

Abla Tannous at 14:50, 10 May 2011

Abla Tannous — Tue, 10 May 2011 14:50:17 GMT

←Older revision		Revision as of 14:50, 10 May 2011
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	One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].		One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
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-	{{Clear}}
-	<applet load='2GTG' size='[450,338]' frame='true' align='right'
-	caption='Saposin C domain of prosaposin ' scene='User:Abla Tannous/Sandbox_1/Loadedfrompdb/4'/>
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Abla Tannous at 14:49, 10 May 2011

Abla Tannous — Tue, 10 May 2011 14:49:22 GMT

←Older revision		Revision as of 14:49, 10 May 2011
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	One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].		One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
		+
		+	{{Clear}}
		+	<applet load='2GTG' size='[450,338]' frame='true' align='right'
		+	caption='Saposin C domain of prosaposin ' scene='User:Abla Tannous/Sandbox_1/Loadedfrompdb/4'/>
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Abla Tannous at 14:40, 10 May 2011

Abla Tannous — Tue, 10 May 2011 14:40:46 GMT

←Older revision		Revision as of 14:40, 10 May 2011
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		+	One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].
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		+	== Saposin C domain of prosaposin ==
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	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1		<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1

Abla Tannous at 03:45, 10 May 2011

Abla Tannous — Tue, 10 May 2011 03:45:26 GMT

←Older revision		Revision as of 03:45, 10 May 2011
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	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>		<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>

-	Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal enzymes (1. Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins(1). Deficiency of UGT1 causes defects in prosaposin maturation(1). Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins(2). The saposin motif is characterized by six cysteines that form three intramolecular disulfide bonds(2). In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic α-helices, where the third helix shows a highly localized kink (2).	+	Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal enzymes (1). Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins(1). Deficiency of UGT1 causes defects in prosaposin maturation(1). Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins(2). The saposin motif is characterized by six cysteines that form three intramolecular disulfide bonds(2). In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic α-helices, where the third helix shows a highly localized kink (2).

Abla Tannous at 03:42, 10 May 2011

Abla Tannous — Tue, 10 May 2011 03:42:14 GMT

←Older revision		Revision as of 03:42, 10 May 2011
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-	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1~~</scene>~~	+	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1

Abla Tannous at 03:35, 10 May 2011

Abla Tannous — Tue, 10 May 2011 03:35:04 GMT

←Older revision		Revision as of 03:35, 10 May 2011
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-	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='~~Insert optional scene name here'~~ /~~>Molecular Playground~~/~~Saposin~~ C	+	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>
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	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>		<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>

Abla Tannous at 03:33, 10 May 2011

Abla Tannous — Tue, 10 May 2011 03:33:30 GMT

←Older revision		Revision as of 03:33, 10 May 2011
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-	Molecular Playground/Saposin C	+	<Structure load='2GTG' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />Molecular Playground/Saposin C

	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>		<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>

Abla Tannous at 03:24, 10 May 2011

Abla Tannous — Tue, 10 May 2011 03:24:33 GMT

←Older revision		Revision as of 03:24, 10 May 2011
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	Molecular Playground/Saposin C		Molecular Playground/Saposin C

-	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The ~~Saposin~~ C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>	+	<scene name='User:Abla_Tannous/Sandbox_1/Saposin_c/1'> The saposin C domain of prosaposin, an obligate substrate for the ER folding sensor UGT1</scene>

-	Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal ~~enzymes1~~. Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins.1 Deficiency of UGT1 causes defects in prosaposin maturation.1 Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins.2 The saposin motif is characterized by six cysteines that form three intramolecular disulfide bonds. 2 In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic α-helices, where the third helix shows a highly localized kink.2	+	Prosaposin is a precursor of four cofactors, saposins A, B,C and D, which are required for hydrolysis of sphingolipids by lysosomal enzymes (1. Prosaposin contains multiple glycans and was found to be an obligate substrate for the UDP-glucose:glycoprotein glucosyl transferase 1 (UGT1), a folding sensor that resides in the ER and supports folding of secretory proteins(1). Deficiency of UGT1 causes defects in prosaposin maturation(1). Prosaposin is cleaved in the lysosome into the four saposins. The four saposins are members of the larger family of saposin –like proteins(2). The saposin motif is characterized by six cysteines that form three intramolecular disulfide bonds(2). In this representation is shown the saposin C domain of prosaposin. Saposin C adopts a monomeric saposin fold with four amphipathic α-helices, where the third helix shows a highly localized kink (2).