4yvf
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yvf]] is a 2 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=4YVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YVF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4yvf]] is a 2 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=4YVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YVF FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=XFA:2-{[5-CHLORO-2-(4-CHLOROPHENOXY)PHENYL](2-{[2-(METHYLAMINO)ETHYL]AMINO}-2-OXOETHYL)AMINO}-N-(1,3-DIHYDRO-2H-ISOINDOL-2-YL)-N-METHYLACETAMIDE'>XFA</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]] 2.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=XFA:2-{[5-CHLORO-2-(4-CHLOROPHENOXY)PHENYL](2-{[2-(METHYLAMINO)ETHYL]AMINO}-2-OXOETHYL)AMINO}-N-(1,3-DIHYDRO-2H-ISOINDOL-2-YL)-N-METHYLACETAMIDE'>XFA</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=4yvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvf OCA], [https://pdbe.org/4yvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yvf RCSB], [https://www.ebi.ac.uk/pdbsum/4yvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yvf 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=4yvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yvf OCA], [https://pdbe.org/4yvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yvf RCSB], [https://www.ebi.ac.uk/pdbsum/4yvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yvf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref> | [https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Optimization of a new series of S-adenosyl-L-homocysteine hydrolase (AdoHcyase) inhibitors based on non-adenosine analogs led to very potent compounds 14n, 18a, and 18b with IC50 values of 13 +/- 3, 5.0 +/- 2.0, and 8.5 +/- 3.1 nM, respectively. An X-ray crystal structure of AdoHcyase with NAD(+) and 18a showed a novel open form co-crystal structure. 18a in the co-crystals formed intramolecular eight membered ring hydrogen bond formations. A single crystal X-ray structure of 14n also showed an intramolecular eight-membered ring hydrogen bond interaction. | ||
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| - | Discovery and structural analyses of S-adenosyl-L-homocysteine hydrolase inhibitors based on non-adenosine analogs.,Nakao A, Suzuki H, Ueno H, Iwasaki H, Setsuta T, Kashima A, Sunada S Bioorg Med Chem. 2015 Aug 1;23(15):4952-69. doi: 10.1016/j.bmc.2015.05.018. Epub , 2015 May 19. PMID:26037610<ref>PMID:26037610</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4yvf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of S-adenosyl-L-homocysteine hydrolase
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