3ioh: Difference between revisions
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<StructureSection load='3ioh' size='340' side='right'caption='[[3ioh]], [[Resolution|resolution]] 1.25Å' scene=''> | <StructureSection load='3ioh' size='340' side='right'caption='[[3ioh]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ioh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ioh]] 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=3IOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IOH 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]] 1.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3ioh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ioh OCA], [https://pdbe.org/3ioh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ioh RCSB], [https://www.ebi.ac.uk/pdbsum/3ioh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ioh 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=3ioh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ioh OCA], [https://pdbe.org/3ioh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ioh RCSB], [https://www.ebi.ac.uk/pdbsum/3ioh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ioh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jorgensen | [[Category: Jorgensen R]] | ||
[[Category: Palcic | [[Category: Palcic MM]] | ||
[[Category: Pesnot | [[Category: Pesnot T]] | ||
[[Category: Wagner | [[Category: Wagner GK]] | ||
Latest revision as of 10:54, 6 September 2023
Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A)Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A)
Structural highlights
FunctionBGAT_HUMAN This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a new donor analog for galactosyltransferases that locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this unique mode of glycosyltransferase inhibition may also be generally applicable to other members of this important enzyme family. Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.,Pesnot T, Jorgensen R, Palcic MM, Wagner GK Nat Chem Biol. 2010 May;6(5):321-3. Epub 2010 Apr 4. PMID:20364127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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