6wg5
From Proteopedia
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<StructureSection load='6wg5' size='340' side='right'caption='[[6wg5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6wg5' size='340' side='right'caption='[[6wg5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WG5 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg5 OCA], [https://pdbe.org/6wg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wg5 RCSB], [https://www.ebi.ac.uk/pdbsum/6wg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg5 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
- | == Function == | ||
- | [[http://www.uniprot.org/uniprot/ENTP4_HUMAN ENTP4_HUMAN]] Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP. | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles that are major regulators of purinergic signaling. Their intracellular roles, however, have not been clearly defined. NTPDase4 (UDPase, ENTPD4) is a Golgi protein potentially involved in nucleotide recycling as part of protein glycosylation, and is also found in lysosomes, where its purpose is unknown. To further our understanding of NTPDase4 function, we determined its crystal structure. The enzyme adopts a wide open, inactive conformation. Differences in the nucleotide-binding site relative to its homologs could account for its substrate selectivity. The putative membrane-interacting loop of cell-surface NTPDases is drastically altered in NTPDase4, potentially affecting its inter-domain dynamics at the Golgi membrane. This article is protected by copyright. All rights reserved. | ||
- | + | ==See Also== | |
- | + | *[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Gorelik A]] | |
- | [[Category: Gorelik | + | [[Category: Illes K]] |
- | [[Category: Illes | + | [[Category: Labriola JM]] |
- | [[Category: Labriola | + | [[Category: Nagar B]] |
- | [[Category: Nagar | + | |
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Current revision
Human ectonucleoside triphosphate diphosphohydrolase 4 (ENTPD4, NTPDase 4)
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