6qab

From Proteopedia

(Difference between revisions)

Current revision

Human Butyrylcholinesterase in complex with (S)-N-(1-((2-cycloheptylethyl)amino)-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-N,N-dimethylbutan-1-aminium

Structural highlights

6qab is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.49Å
Ligands:	, , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CHLE_HUMAN Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait.

Function

CHLE_HUMAN Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.^[1] ^[2]

Publication Abstract from PubMed

We have identified tryptophan-based selective nanomolar butyrylcholinesterase (BChE) inhibitors. They are defined according to their chemical modularity, novel binding mode revealed by five solved crystal structures with human BChE, low cytotoxicity, and predicted permeability of the blood-brain barrier. Altogether, these factors indicate their potential as unique lead compounds for symptomatic therapy against Alzheimer's disease.

Tryptophan-derived butyrylcholinesterase inhibitors as promising leads against Alzheimer's disease.,Meden A, Knez D, Jukic M, Brazzolotto X, Grsic M, Pislar A, Zahirovic A, Kos J, Nachon F, Svete J, Gobec S, Groselj U Chem Commun (Camb). 2019 Mar 26;55(26):3765-3768. doi: 10.1039/c9cc01330j. PMID:30864579^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chilukuri N, Duysen EG, Parikh K, diTargiani R, Doctor BP, Lockridge O, Saxena A. Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents. Mol Pharmacol. 2009 Sep;76(3):612-7. doi: 10.1124/mol.109.055665. Epub 2009 Jun, 19. PMID:19542320 doi:10.1124/mol.109.055665
↑ Amitay M, Shurki A. The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger. Proteins. 2009 Nov 1;77(2):370-7. doi: 10.1002/prot.22442. PMID:19452557 doi:10.1002/prot.22442
↑ Meden A, Knez D, Jukic M, Brazzolotto X, Grsic M, Pislar A, Zahirovic A, Kos J, Nachon F, Svete J, Gobec S, Groselj U. Tryptophan-derived butyrylcholinesterase inhibitors as promising leads against Alzheimer's disease. Chem Commun (Camb). 2019 Mar 26;55(26):3765-3768. doi: 10.1039/c9cc01330j. PMID:30864579 doi:http://dx.doi.org/10.1039/c9cc01330j

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6qab"

@@ Line 3: / Line 3: @@
 <StructureSection load='6qab' size='340' side='right'caption='[[6qab]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6qab]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QAB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6qab]] 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=6QAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QAB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HUQ:butyl-[(2~{S})-1-(2-cycloheptylethylamino)-3-(1~{H}-indol-3-yl)-1-oxidanylidene-propan-2-yl]-dimethyl-azanium'>HUQ</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.49&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HUQ:butyl-[(2~{S})-1-(2-cycloheptylethylamino)-3-(1~{H}-indol-3-yl)-1-oxidanylidene-propan-2-yl]-dimethyl-azanium'>HUQ</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6qab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qab OCA], [http://pdbe.org/6qab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qab RCSB], [http://www.ebi.ac.uk/pdbsum/6qab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qab 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=6qab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qab OCA], [https://pdbe.org/6qab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qab RCSB], [https://www.ebi.ac.uk/pdbsum/6qab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qab ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN]] Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:[http://omim.org/entry/177400 177400]]. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait.
+[https://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN] Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:[https://omim.org/entry/177400 177400]. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait.
 == Function ==
-[[http://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN]] Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.<ref>PMID:19542320</ref> <ref>PMID:19452557</ref>
+[https://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN] Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.<ref>PMID:19542320</ref> <ref>PMID:19452557</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 6qab" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Butyrylcholinesterase 3D structures|Butyrylcholinesterase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cholinesterase]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Brazzolotto, X]]
+[[Category: Brazzolotto X]]
-[[Category: Gobec, S]]
+[[Category: Gobec S]]
-[[Category: Harst, M]]
+[[Category: Harst M]]
-[[Category: Knez, D]]
+[[Category: Knez D]]
-[[Category: Nachon, F]]
+[[Category: Nachon F]]
-[[Category: Butyrylcholinesterase]]
-[[Category: Complex]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]

6qab

From Proteopedia

Current revision

Human Butyrylcholinesterase in complex with (S)-N-(1-((2-cycloheptylethyl)amino)-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-N,N-dimethylbutan-1-aminium

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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