4kc2
From Proteopedia
(Difference between revisions)
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<StructureSection load='4kc2' size='340' side='right' caption='[[4kc2]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4kc2' size='340' side='right' caption='[[4kc2]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4kc2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4kc2]] 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=4KC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KC2 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHE:OCTYL+2-O-(6-DEOXY-ALPHA-L-GALACTOPYRANOSYL)-BETA-D-GALACTOPYRANOSIDE'>BHE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=WS2:6-(1-BETA-D-GALACTOPYRANOSYLOXYMETHYL)-N-(5-DEOXYLURIDINE-5-YL)PICOLINAMIDE'>WS2</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHE:OCTYL+2-O-(6-DEOXY-ALPHA-L-GALACTOPYRANOSYL)-BETA-D-GALACTOPYRANOSIDE'>BHE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=WS2:6-(1-BETA-D-GALACTOPYRANOSYLOXYMETHYL)-N-(5-DEOXYLURIDINE-5-YL)PICOLINAMIDE'>WS2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kc1|4kc1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kc1|4kc1]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4kc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc2 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=4kc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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. | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A series of ten glycosyltransferase inhibitors has been designed and synthesized by using pyridine as a pyrophosphate surrogate. The series was prepared by conjugation of carbohydrate, pyridine, and nucleoside building blocks by using a combination of glycosylation, the Staudinger-Vilarrasa amide-bond formation, and azide-alkyne click chemistry. The compounds were evaluated as inhibitors of five metal-dependent galactosyltransferases. Crystallographic analyses of three inhibitors complexed in the active site of one of the enzymes confirmed that the pyridine moiety chelates the Mn(2+) ion causing a slight displacement (2 A) from its original position. The carbohydrate head group occupies a different position than in the natural uridine diphosphate (UDP)-Gal substrate with little interaction with the enzyme. | ||
| + | |||
| + | Design of glycosyltransferase inhibitors: pyridine as a pyrophosphate surrogate.,Wang S, Cuesta-Seijo JA, Lafont D, Palcic MM, Vidal S Chemistry. 2013 Nov 4;19(45):15346-57. doi: 10.1002/chem.201301871. Epub 2013 Sep, 23. PMID:24108680<ref>PMID:24108680</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Cuesta-Seijo, J A]] | [[Category: Cuesta-Seijo, J A]] | ||
[[Category: Lafont, D]] | [[Category: Lafont, D]] | ||
Revision as of 11:29, 4 March 2015
Structure of the blood group glycosyltransferase AAglyB in complex with a pyridine inhibitor as a neutral pyrophosphate surrogate
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