5fql: Difference between revisions
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==Insights into Hunter syndrome from the structure of iduronate-2- sulfatase== | ==Insights into Hunter syndrome from the structure of iduronate-2- sulfatase== | ||
<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. 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 [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> | ||
</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='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> | ||
<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='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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5fql" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5fql" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Sulfatase|Sulfatase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Iduronate-2-sulfatase]] | [[Category: Iduronate-2-sulfatase]] | ||
[[Category: Large Structures]] | |||
[[Category: Bunkoczi, G]] | [[Category: Bunkoczi, G]] | ||
[[Category: Deane, J E]] | [[Category: Deane, J E]] | ||
Revision as of 10:35, 23 October 2019
Insights into Hunter syndrome from the structure of iduronate-2- sulfataseInsights into Hunter syndrome from the structure of iduronate-2- sulfatase
Structural highlights
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 PubMedHunter 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 AlsoReferences
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