3wez - Revision history

OCA at 13:07, 8 November 2023

2023-11-08T13:07:45Z

←Older revision		Revision as of 13:07, 8 November 2023
Line 3:		Line 3:
	<StructureSection load='3wez' size='340' side='right'caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>		<StructureSection load='3wez' size='340' side='right'caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wez]] is a 4 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=3WEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wez]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N8V:(1S,2S,3S,6R)-4-(HYDROXYMETHYL)-6-(OCTYLAMINO)CYCLOHEX-4-ENE-1,2,3-TRIOL'>N8V</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.11Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wf0\|3wf0]], [[3wf1\|3wf1]], [[3wf2\|3wf2]], [[3wf3\|3wf3]], [[3wf4\|3wf4]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N8V:(1S,2S,3S,6R)-4-(HYDROXYMETHYL)-6-(OCTYLAMINO)CYCLOHEX-4-ENE-1,2,3-TRIOL'>N8V</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ELNR1, GLB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [https://pdbe.org/3wez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [https://www.ebi.ac.uk/pdbsum/3wez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wez 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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [https://pdbe.org/3wez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [https://www.ebi.ac.uk/pdbsum/3wez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wez ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>	+	[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>	+	[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>

	==See Also==		==See Also==
Line 21:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Beta-galactosidase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ohto, U]]	+	[[Category: Ohto U]]
-	[[Category: Shimizu, T]]	+	[[Category: Shimizu T]]
-	[[Category: Suzuki, H]]	+	[[Category: Suzuki H]]
-	~~[[Category: Glycosyl hydrolase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Tim-barrel domain~~]]	+

OCA at 05:34, 3 August 2022

2022-08-03T05:34:11Z

←Older revision		Revision as of 05:34, 3 August 2022
Line 1:		Line 1:

	==Crystal structure of human beta-galactosidase in complex with NOEV==		==Crystal structure of human beta-galactosidase in complex with NOEV==
-	<StructureSection load='3wez' size='340' side='right' caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>	+	<StructureSection load='3wez' size='340' side='right'caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wez]] is a 4 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=3WEZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3WEZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wez]] is a 4 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=3WEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N8V:(1S,2S,3S,6R)-4-(HYDROXYMETHYL)-6-(OCTYLAMINO)CYCLOHEX-4-ENE-1,2,3-TRIOL'>N8V</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N8V:(1S,2S,3S,6R)-4-(HYDROXYMETHYL)-6-(OCTYLAMINO)CYCLOHEX-4-ENE-1,2,3-TRIOL'>N8V</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wf0\|3wf0]], [[3wf1\|3wf1]], [[3wf2\|3wf2]], [[3wf3\|3wf3]], [[3wf4\|3wf4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wf0\|3wf0]], [[3wf1\|3wf1]], [[3wf2\|3wf2]], [[3wf3\|3wf3]], [[3wf4\|3wf4]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ELNR1, GLB1 ([~~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">ELNR1, GLB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [~~http~~://pdbe.org/3wez PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3wez PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3wez 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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [https://pdbe.org/3wez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [https://www.ebi.ac.uk/pdbsum/3wez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wez ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[~~http~~://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[~~http~~://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[~~http~~://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[~~http~~://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>	+	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>	+	[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>

	==See Also==		==See Also==
-	*[[Galactosidase\|Galactosidase]]	+	*[[Galactosidase 3D structures\|Galactosidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 23:
	[[Category: Beta-galactosidase]]		[[Category: Beta-galactosidase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ohto, U]]		[[Category: Ohto, U]]
	[[Category: Shimizu, T]]		[[Category: Shimizu, T]]

OCA at 08:56, 11 August 2016

2016-08-11T08:56:32Z

←Older revision		Revision as of 08:56, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human beta-galactosidase in complex with NOEV==		==Crystal structure of human beta-galactosidase in complex with NOEV==
	<StructureSection load='3wez' size='340' side='right' caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>		<StructureSection load='3wez' size='340' side='right' caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ELNR1, GLB1 ([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">ELNR1, GLB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [http://www.ebi.ac.uk/pdbsum/3wez 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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [http://pdbe.org/3wez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [http://www.ebi.ac.uk/pdbsum/3wez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wez ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 13:		Line 14:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>		[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
		+
		+	==See Also==
		+	*[[Galactosidase\|Galactosidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:09, 4 January 2015

2015-01-04T11:09:53Z

←Older revision		Revision as of 11:09, 4 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_3wez\| PDB=3wez \| SCENE= }}~~	+	==Crystal structure of human beta-galactosidase in complex with NOEV==
-	===Crystal structure of human beta-galactosidase in complex with NOEV===	+	<StructureSection load='3wez' size='340' side='right' caption='[[3wez]], [[Resolution\|resolution]] 2.11Å' scene=''>
-		+	== Structural highlights ==
-	==Disease==	+	<table><tr><td colspan='2'>[[3wez]] is a 4 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=3WEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WEZ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=N8V:(1S,2S,3S,6R)-4-(HYDROXYMETHYL)-6-(OCTYLAMINO)CYCLOHEX-4-ENE-1,2,3-TRIOL'>N8V</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wf0\|3wf0]], [[3wf1\|3wf1]], [[3wf2\|3wf2]], [[3wf3\|3wf3]], [[3wf4\|3wf4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ELNR1, GLB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=3wez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wez OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wez RCSB], [http://www.ebi.ac.uk/pdbsum/3wez PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[http://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[http://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[http://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[http://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>		[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[http://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[http://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[http://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[http://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>		[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	~~[[3wez]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEZ OCA].~~	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Beta-galactosidase]]		[[Category: Beta-galactosidase]]
-	[[Category: Ohto, U.]]	+	[[Category: Human]]
-	[[Category: Shimizu, T.]]	+	[[Category: Ohto, U]]
-	[[Category: Suzuki, H.]]	+	[[Category: Shimizu, T]]
		+	[[Category: Suzuki, H]]
	[[Category: Glycosyl hydrolase]]		[[Category: Glycosyl hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Tim-barrel domain]]		[[Category: Tim-barrel domain]]

OCA at 07:48, 23 April 2014

2014-04-23T07:48:52Z

←Older revision		Revision as of 07:48, 23 April 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3wez\| PDB=3wez \| SCENE= }}
		+	===Crystal structure of human beta-galactosidase in complex with NOEV===

-	The entry ~~3wez~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[http://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> GM1-gangliosidosis 2 (GM1G2) [MIM:[http://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref> GM1-gangliosidosis 3 (GM1G3) [MIM:[http://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref> Mucopolysaccharidosis 4B (MPS4B) [MIM:[http://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>

-	~~Authors~~: ~~Suzuki, H~~., ~~Ohto~~, U., ~~Shimizu~~, T.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref> Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>

-	~~Description: Crystal~~ structure ~~of human beta~~-galactosidase ~~in complex with NOEV~~	+	==About this Structure==
		+	[[3wez]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEZ OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Beta-galactosidase]]
		+	[[Category: Ohto, U.]]
		+	[[Category: Shimizu, T.]]
		+	[[Category: Suzuki, H.]]
		+	[[Category: Glycosyl hydrolase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Tim-barrel domain]]

OCA at 08:07, 2 April 2014

2014-04-02T08:07:13Z

←Older revision		Revision as of 08:07, 2 April 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3wez is ON HOLD	+	The entry 3wez is ON HOLD until Paper Publication

	Authors: Suzuki, H., Ohto, U., Shimizu, T.		Authors: Suzuki, H., Ohto, U., Shimizu, T.

-	Description: Crystal structure of human beta-galactosidase in complex with ~~NOEV~~ NOEV	+	Description: Crystal structure of human beta-galactosidase in complex with NOEV

OCA at 19:37, 7 August 2013

2013-08-07T19:37:17Z

←Older revision		Revision as of 19:37, 7 August 2013
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	The entry 3wez is ON HOLD		The entry 3wez is ON HOLD

-	Authors: Suzuki, H., Ohto, U., Shimizu, T	+	Authors: Suzuki, H., Ohto, U., Shimizu, T.

	Description: Crystal structure of human beta-galactosidase in complex with NOEV NOEV		Description: Crystal structure of human beta-galactosidase in complex with NOEV NOEV

OCA: Protected "3wez" [edit=sysop:move=sysop]

2013-07-24T11:56:57Z

Protected "3wez" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:56, 24 July 2013

OCA: New page: '''Unreleased structure''' The entry 3wez is ON HOLD Authors: Suzuki, H., Ohto, U., Shimizu, T Description: Crystal structure of human beta-galactosidase in complex with NOEV NOEV

2013-07-24T11:56:56Z

New page: '''Unreleased structure''' The entry 3wez is ON HOLD Authors: Suzuki, H., Ohto, U., Shimizu, T Description: Crystal structure of human beta-galactosidase in complex with NOEV NOEV

New page

'''Unreleased structure'''

The entry 3wez is ON HOLD

Authors: Suzuki, H., Ohto, U., Shimizu, T

Description: Crystal structure of human beta-galactosidase in complex with NOEV NOEV