2ag2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ag2]] is a 3 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=2AG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AG2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ag2]] is a 3 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=2AG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AG2 FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CH5:2-(((R)-2,3-DIHYDROXYPROPYL)PHOSPHORYLOXY)-N,N,N-TRIMETHYLETHANAMINIUM'>CH5</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=LP3:(7R)-4,7-DIHYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOSAN-1-AMINIUM+4-OXIDE'>LP3</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CH5:2-(((R)-2,3-DIHYDROXYPROPYL)PHOSPHORYLOXY)-N,N,N-TRIMETHYLETHANAMINIUM'>CH5</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=LP3:(7R)-4,7-DIHYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOSAN-1-AMINIUM+4-OXIDE'>LP3</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g13|1g13]], [[1pub|1pub]], [[1pu5|1pu5]], [[1tjj|1tjj]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g13|1g13]], [[1pub|1pub]], [[1pu5|1pu5]], [[1tjj|1tjj]]</td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GM2A ([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">GM2A ([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=2ag2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ag2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ag2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ag2 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=2ag2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ag2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ag2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ag2 PDBsum]</span></td></tr> |
- | <table> | + | </table> |
== Disease == | == Disease == | ||
[[http://www.uniprot.org/uniprot/SAP3_HUMAN SAP3_HUMAN]] Defects in GM2A are the cause of GM2-gangliosidosis type AB (GM2GAB) [MIM:[http://omim.org/entry/272750 272750]]; also known as Tay-Sachs disease AB variant. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2GAB is characterized by GM2 gangliosides accumulation in the presence of both hexosaminidase A and B.<ref>PMID:1915858</ref> <ref>PMID:8244332</ref> <ref>PMID:8900233</ref> | [[http://www.uniprot.org/uniprot/SAP3_HUMAN SAP3_HUMAN]] Defects in GM2A are the cause of GM2-gangliosidosis type AB (GM2GAB) [MIM:[http://omim.org/entry/272750 272750]]; also known as Tay-Sachs disease AB variant. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2GAB is characterized by GM2 gangliosides accumulation in the presence of both hexosaminidase A and B.<ref>PMID:1915858</ref> <ref>PMID:8244332</ref> <ref>PMID:8900233</ref> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Lee, S | + | [[Category: Lee, S]] |
- | [[Category: Mi, L Z | + | [[Category: Mi, L Z]] |
- | [[Category: Rastinejad, F | + | [[Category: Rastinejad, F]] |
- | [[Category: Wright, C S | + | [[Category: Wright, C S]] |
[[Category: Lipid acyl chain stacking]] | [[Category: Lipid acyl chain stacking]] | ||
[[Category: Lipid binding protein]] | [[Category: Lipid binding protein]] | ||
[[Category: Packaging]] | [[Category: Packaging]] | ||
[[Category: Phospholipid-protein complex]] | [[Category: Phospholipid-protein complex]] |
Revision as of 09:22, 8 January 2015
Crystal Structure Analysis of GM2-activator protein complexed with Phosphatidylcholine
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