2r1q - Revision history

OCA at 04:11, 2 July 2021

OCA — Fri, 02 Jul 2021 04:11:37 GMT

←Older revision		Revision as of 04:11, 2 July 2021
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	==Crystal Structure of Iodinated Human Saposin D in Space Group C2221==		==Crystal Structure of Iodinated Human Saposin D in Space Group C2221==
-	<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='2r1q' size='340' side='right'caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [~~http~~://pdbe.org/2r1q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2r1q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2r1q ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [https://pdbe.org/2r1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [https://www.ebi.ac.uk/pdbsum/2r1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r1q ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[~~http~~://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref> <ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[~~http~~://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[~~http~~://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref> <ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[~~http~~://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).	+	[[https://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[https://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref> <ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[https://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[https://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref> <ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[https://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymic proteins: the sphingolipids activator proteins (coproteins). Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).	+	[[https://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymic proteins: the sphingolipids activator proteins (coproteins). Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/2r1q_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/2r1q_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 2r1q" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2r1q" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Saposin\|Saposin]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Maier, T]]		[[Category: Maier, T]]
	[[Category: Rossman, M]]		[[Category: Rossman, M]]

OCA at 07:40, 25 October 2017

OCA — Wed, 25 Oct 2017 07:40:51 GMT

←Older revision		Revision as of 07:40, 25 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of Iodinated Human Saposin D in Space Group C2221==		==Crystal Structure of Iodinated Human Saposin D in Space Group C2221==
	<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://pdbe.org/2r1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://pdbe.org/2r1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r1q ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 2r1q" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2r1q" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Saposin\|Saposin]]
	== References ==		== References ==
	<references/>		<references/>
Line 43:		Line 41:
	[[Category: Saenger, W]]		[[Category: Saenger, W]]
	[[Category: Activator protein]]		[[Category: Activator protein]]
		+	[[Category: Alternative splicing]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Gaucher disease]]		[[Category: Gaucher disease]]

OCA at 11:47, 9 February 2016

OCA — Tue, 09 Feb 2016 11:47:30 GMT

←Older revision		Revision as of 11:47, 9 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r1q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:55, 10 September 2015

OCA — Thu, 10 Sep 2015 21:55:32 GMT

←Older revision		Revision as of 21:55, 10 September 2015
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	<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://pdbe.org/2r1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2r1q" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Maier, T]]		[[Category: Maier, T]]
	[[Category: Rossman, M]]		[[Category: Rossman, M]]

OCA at 18:07, 19 January 2015

OCA — Mon, 19 Jan 2015 18:07:04 GMT

←Older revision		Revision as of 18:07, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[http://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref> <ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[http://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[http://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref> <ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[http://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).		[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[http://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref> <ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[http://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[http://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref> <ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[http://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Maier, T.]]	+	[[Category: Maier, T]]
-	[[Category: Rossman, M.]]	+	[[Category: Rossman, M]]
-	[[Category: Saenger, W.]]	+	[[Category: Saenger, W]]
	[[Category: Activator protein]]		[[Category: Activator protein]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]

OCA at 20:09, 30 September 2014

OCA — Tue, 30 Sep 2014 20:09:55 GMT

←Older revision		Revision as of 20:09, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2r1q\| PDB=2r1q \| SCENE= }}~~	+	==Crystal Structure of Iodinated Human Saposin D in Space Group C2221==
-	===Crystal Structure of Iodinated Human Saposin D in Space Group C2221===	+	<StructureSection load='2r1q' size='340' side='right' caption='[[2r1q]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_18462685}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R1Q FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2z9a\|2z9a]], [[2qyp\|2qyp]], [[2r0r\|2r0r]], [[2rb3\|2rb3]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PSAP, GLBA, SAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r1q RCSB], [http://www.ebi.ac.uk/pdbsum/2r1q PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[http://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref> <ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[http://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[http://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref> <ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[http://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymic proteins: the sphingolipids activator proteins (coproteins). Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/2r1q_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers. This form of SapC dimer supports the "clip-on" model for SapC-induced vesicle fusion. In addition, we present the crystal structure of SapD in two crystal forms. They reveal the monomer-monomer interface for the SapD dimer, which was confirmed in solution by analytical ultracentrifugation. The crystal structure of SapD suggests that side chains of Lys10 and Arg17 are involved in initial association with the preferred anionic biological membranes by forming salt bridges with sulfate or phosphate lipid headgroups.

-	~~==Disease==~~	+	Crystal structures of human saposins C andD: implications for lipid recognition and membrane interactions.,Rossmann M, Schultz-Heienbrok R, Behlke J, Remmel N, Alings C, Sandhoff K, Saenger W, Maier T Structure. 2008 May;16(5):809-17. PMID:18462685<ref>PMID:18462685</ref>
-	~~[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause~~ of ~~combined saposin deficiency (CSAPD) [MIM~~:~~[http://omim~~.~~org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins~~, ~~leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref><ref>PMID:11309366</ref> Defects in PSAP saposin~~-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[http://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, ~~demyelination~~, ~~periventricular white matter abnormalities~~, ~~peripheral neuropathy. Additional neurological features include dysarthria~~, ~~ataxic gait~~, ~~psychomotr regression~~, ~~seizures, cognitive decline and spastic quadriparesis~~. ~~Defects in PSAP saposin-C region are the cause of atypical Gaucher disease~~ (~~AGD~~) ~~[MIM~~:~~[http://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide~~-~~beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder~~.~~<ref>~~PMID:~~2060627</ref>~~<ref>PMID:~~17919309~~</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[http://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~//www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, ~~non-enzymic proteins: the sphingolipids activator proteins (coproteins). Saposin-A and saposin-C stimulate the hydrolysis~~ of ~~glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with~~ the ~~enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate~~. ~~Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3~~.~~1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates~~ of ~~the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12)~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[2r1q]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA].~~	+

	==See Also==		==See Also==
	*[[Saposin\|Saposin]]		*[[Saposin\|Saposin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:018462685</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Maier, T.]]		[[Category: Maier, T.]]

OCA at 06:55, 25 March 2013

OCA — Mon, 25 Mar 2013 06:55:59 GMT

←Older revision		Revision as of 06:55, 25 March 2013
Line 1:		Line 1:
-	[[Image:2r1q.png\|left\|200px]]
-
	{{STRUCTURE_2r1q\| PDB=2r1q \| SCENE= }}		{{STRUCTURE_2r1q\| PDB=2r1q \| SCENE= }}
-
	===Crystal Structure of Iodinated Human Saposin D in Space Group C2221===		===Crystal Structure of Iodinated Human Saposin D in Space Group C2221===
		+	{{ABSTRACT_PUBMED_18462685}}

-	~~{{ABSTRACT_PUBMED_18462685}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] Defects in PSAP are the cause of combined saposin deficiency (CSAPD) [MIM:[http://omim.org/entry/611721 611721]]; also known as prosaposin deficiency. CSAPD is due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.<ref>PMID:1371116</ref><ref>PMID:11309366</ref> Defects in PSAP saposin-B region are the cause of leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB) [MIM:[http://omim.org/entry/249900 249900]]. MLD-SAPB is an atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotr regression, seizures, cognitive decline and spastic quadriparesis. Defects in PSAP saposin-C region are the cause of atypical Gaucher disease (AGD) [MIM:[http://omim.org/entry/610539 610539]]. Affected individuals have marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease, a lysosomal storage disorder.<ref>PMID:2060627</ref><ref>PMID:17919309</ref> Defects in PSAP saposin-A region are the cause of atypical Krabbe disease (AKRD) [MIM:[http://omim.org/entry/611722 611722]]. AKRD is a disorder of galactosylceramide metabolism. AKRD features include progressive encephalopathy and abnormal myelination in the cerebral white matter resembling Krabbe disease.<ref>PMID:15773042</ref> Note=Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SAP_HUMAN SAP_HUMAN]] The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymic proteins: the sphingolipids activator proteins (coproteins). Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018462685</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018462685</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Maier, T.]]		[[Category: Maier, T.]]

OCA at 13:44, 20 October 2012

OCA — Sat, 20 Oct 2012 13:44:08 GMT

←Older revision		Revision as of 13:44, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2r1q]] is a 1 chain structure ~~of [[Saposin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA].	+	[[2r1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA].

	==See Also==		==See Also==

OCA: Protected "2r1q" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 12:56:18 GMT

Protected "2r1q" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:56, 26 July 2012

OCA at 12:56, 26 July 2012

OCA — Thu, 26 Jul 2012 12:56:17 GMT

←Older revision		Revision as of 12:56, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2r1q.png\|left\|200px]]		[[Image:2r1q.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2r1q", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2r1q\| PDB=2r1q \| SCENE= }}		{{STRUCTURE_2r1q\| PDB=2r1q \| SCENE= }}

	===Crystal Structure of Iodinated Human Saposin D in Space Group C2221===		===Crystal Structure of Iodinated Human Saposin D in Space Group C2221===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18462685}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18462685 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18462685}}		{{ABSTRACT_PUBMED_18462685}}

	==About this Structure==		==About this Structure==
-	~~2R1Q~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA].	+	[[2r1q]] is a 1 chain structure of [[Saposin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R1Q OCA].
		+
		+	==See Also==
		+	*[[Saposin\|Saposin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18462685~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018462685</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Maier, T.]]		[[Category: Maier, T.]]
Line 29:		Line 20:
	[[Category: Saenger, W.]]		[[Category: Saenger, W.]]
	[[Category: Activator protein]]		[[Category: Activator protein]]
-	[[Category: Alternative splicing]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Gaucher disease]]		[[Category: Gaucher disease]]
Line 41:		Line 31:
	[[Category: Saposin]]		[[Category: Saposin]]
	[[Category: Sphingolipid metabolism]]		[[Category: Sphingolipid metabolism]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:32:06 2009''