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| | <StructureSection load='5fql' size='340' side='right'caption='[[5fql]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5fql' size='340' side='right'caption='[[5fql]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fql]] 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=5FQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FQL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fql]] is a 1 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=5FQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FQL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALS:(3S)-3-(SULFOOXY)-L-SERINE'>ALS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALS:(3S)-3-(SULFOOXY)-L-SERINE'>ALS</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Iduronate-2-sulfatase Iduronate-2-sulfatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.13 3.1.6.13] </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=5fql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fql OCA], [https://pdbe.org/5fql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fql RCSB], [https://www.ebi.ac.uk/pdbsum/5fql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fql ProSAT]</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=5fql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fql OCA], [http://pdbe.org/5fql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fql RCSB], [http://www.ebi.ac.uk/pdbsum/5fql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fql ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/IDS_HUMAN IDS_HUMAN]] Mucopolysaccharidosis type 2, attenuated form;Mucopolysaccharidosis type 2, severe form. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/IDS_HUMAN IDS_HUMAN] Mucopolysaccharidosis type 2, attenuated form;Mucopolysaccharidosis type 2, severe form. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IDS_HUMAN IDS_HUMAN]] Required for the lysosomal degradation of heparan sulfate and dermatan sulfate. | + | [https://www.uniprot.org/uniprot/IDS_HUMAN IDS_HUMAN] Required for the lysosomal degradation of heparan sulfate and dermatan sulfate. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Sulfatase|Sulfatase]] | + | *[[Sulfatase 3D structures|Sulfatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Iduronate-2-sulfatase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bunkoczi, G]] | + | [[Category: Bunkoczi G]] |
| - | [[Category: Deane, J E]] | + | [[Category: Deane JE]] |
| - | [[Category: Demydchuk, M]] | + | [[Category: Demydchuk M]] |
| - | [[Category: Hill, C H]] | + | [[Category: Hill CH]] |
| - | [[Category: Marchesan, D]] | + | [[Category: Marchesan D]] |
| - | [[Category: Read, R J]] | + | [[Category: Read RJ]] |
| - | [[Category: Stein, P E]] | + | [[Category: Stein PE]] |
| - | [[Category: Zhou, A]] | + | [[Category: Zhou A]] |
| - | [[Category: Hunter syndrome]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
5fql is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
IDS_HUMAN Mucopolysaccharidosis type 2, attenuated form;Mucopolysaccharidosis type 2, severe form. The disease is caused by mutations affecting the gene represented in this entry.
Function
IDS_HUMAN Required for the lysosomal degradation of heparan sulfate and dermatan sulfate.
Publication Abstract from PubMed
Hunter syndrome is a rare but devastating childhood disease caused by mutations in the IDS gene encoding iduronate-2-sulfatase, a crucial enzyme in the lysosomal degradation pathway of dermatan sulfate and heparan sulfate. These complex glycosaminoglycans have important roles in cell adhesion, growth, proliferation and repair, and their degradation and recycling in the lysosome is essential for cellular maintenance. A variety of disease-causing mutations have been identified throughout the IDS gene. However, understanding the molecular basis of the disease has been impaired by the lack of structural data. Here, we present the crystal structure of human IDS with a covalently bound sulfate ion in the active site. This structure provides essential insight into multiple mechanisms by which pathogenic mutations interfere with enzyme function, and a compelling explanation for severe Hunter syndrome phenotypes. Understanding the structural consequences of disease-associated mutations will facilitate the identification of patients that may benefit from specific tailored therapies.
Insights into Hunter syndrome from the structure of iduronate-2-sulfatase.,Demydchuk M, Hill CH, Zhou A, Bunkoczi G, Stein PE, Marchesan D, Deane JE, Read RJ Nat Commun. 2017 Jun 8;8:15786. doi: 10.1038/ncomms15786. PMID:28593992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Demydchuk M, Hill CH, Zhou A, Bunkoczi G, Stein PE, Marchesan D, Deane JE, Read RJ. Insights into Hunter syndrome from the structure of iduronate-2-sulfatase. Nat Commun. 2017 Jun 8;8:15786. doi: 10.1038/ncomms15786. PMID:28593992 doi:http://dx.doi.org/10.1038/ncomms15786
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