4o1l - Revision history

OCA at 08:57, 20 March 2024

OCA — Wed, 20 Mar 2024 08:57:28 GMT

←Older revision		Revision as of 08:57, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o1l]] 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=4O1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1L FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o1l]] 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=4O1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [https://pdbe.org/4o1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [https://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l 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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [https://pdbe.org/4o1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [https://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN] ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.		[https://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN] ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Adenosine kinase (ADK) from Mycobacterium tuberculosis (Mtb) was selected as a target for design of antimycobacterial nucleosides. Screening of 7-(het)aryl-7-deazaadenine ribonucleosides with Mtb and human (h) ADKs and testing with wild-type and drug-resistant Mtb strains identified specific inhibitors of Mtb ADK with micromolar antimycobacterial activity and low cytotoxicity. X-ray structures of complexes of Mtb and hADKs with 7-ethynyl-7-deazaadenosine showed differences in inhibitor interactions in the adenosine binding sites. 1D (1)H STD NMR experiments revealed that these inhibitors are readily accommodated into the ATP and adenosine binding sites of Mtb ADK, whereas they bind preferentially into the adenosine site of hADK. Occupation of the Mtb ADK ATP site with inhibitors and formation of catalytically less competent semiopen conformation of MtbADK after inhibitor binding in the adenosine site explain the lack of phosphorylation of 7-substituted-7-deazaadenosines. Semiempirical quantum mechanical analysis confirmed different affinity of nucleosides for the Mtb ADK adenosine and ATP sites.
-
-	Structural Basis for Inhibition of Mycobacterial and Human Adenosine Kinase by 7-Substituted 7-(Het)aryl-7-deazaadenine Ribonucleosides.,Snasel J, Naus P, Dostal J, Hnizda A, Fanfrlik J, Brynda J, Bourderioux A, Dusek M, Dvorakova H, Stolarikova J, Zabranska H, Pohl R, Konecny P, Dzubak P, Votruba I, Hajduch M, Rezacova P, Veverka V, Hocek M, Pichova I J Med Chem. 2014 Oct 23;57(20):8268-79. doi: 10.1021/jm500497v. Epub 2014 Oct 8. PMID:25259627<ref>PMID:25259627</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4o1l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:51, 18 January 2023

OCA — Wed, 18 Jan 2023 08:51:37 GMT

←Older revision		Revision as of 08:51, 18 January 2023
Line 3:		Line 3:
	<StructureSection load='4o1l' size='340' side='right'caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4o1l' size='340' side='right'caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o1l]] is a 2 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=4O1L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O1L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o1l]] 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=4O1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [https://pdbe.org/4o1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [https://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [~~http~~://pdbe.org/4o1l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN]] Defects in ADK are the cause of hypermethioninemia due to adenosine kinase deficiency (HMAKD) [MIM:[~~http~~://omim.org/entry/614300 614300]]. A metabolic disorder characterized by global developmental delay, early-onset seizures, mild dysmorphic features, and characteristic biochemical anomalies, including persistent hypermethioninemia with increased levels of S-adenosylmethionine and S-adenosylhomocysteine. Homocysteine levels are typically normal.<ref>PMID:21963049</ref>	+	[https://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN] Defects in ADK are the cause of hypermethioninemia due to adenosine kinase deficiency (HMAKD) [MIM:[https://omim.org/entry/614300 614300]. A metabolic disorder characterized by global developmental delay, early-onset seizures, mild dysmorphic features, and characteristic biochemical anomalies, including persistent hypermethioninemia with increased levels of S-adenosylmethionine and S-adenosylhomocysteine. Homocysteine levels are typically normal.<ref>PMID:21963049</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN]] ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.	+	[https://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN] ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Adenosine kinase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brynda, J]]	+	[[Category: Brynda J]]
-	[[Category: Dostal, J]]	+	[[Category: Dostal J]]
-	[[Category: Hodcek, M]]	+	[[Category: Hodcek M]]
-	[[Category: Pichova, I]]	+	[[Category: Pichova I]]
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 08:12, 10 April 2019

OCA — Wed, 10 Apr 2019 08:12:19 GMT

←Older revision		Revision as of 08:12, 10 April 2019
Line 1:		Line 1:

	==Human Adenosine Kinase in complex with inhibitor==		==Human Adenosine Kinase in complex with inhibitor==
-	<StructureSection load='4o1l' size='340' side='right' caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4o1l' size='340' side='right'caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o1l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o1l]] is a 2 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=4O1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1L FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [http://pdbe.org/4o1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [http://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [http://pdbe.org/4o1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [http://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</span></td></tr>
Line 24:		Line 25:

	==See Also==		==See Also==
-	*[[Adenosine kinase\|Adenosine kinase]]	+	*[[Adenosine kinase 3D structures\|Adenosine kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Adenosine kinase]]		[[Category: Adenosine kinase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Brynda, J]]		[[Category: Brynda, J]]
	[[Category: Dostal, J]]		[[Category: Dostal, J]]

OCA at 10:45, 11 August 2016

OCA — Thu, 11 Aug 2016 10:45:07 GMT

←Older revision		Revision as of 10:45, 11 August 2016
Line 1:		Line 1:
		+
	==Human Adenosine Kinase in complex with inhibitor==		==Human Adenosine Kinase in complex with inhibitor==
	<StructureSection load='4o1l' size='340' side='right' caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4o1l' size='340' side='right' caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [http://www.ebi.ac.uk/pdbsum/4o1l 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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [http://pdbe.org/4o1l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [http://www.ebi.ac.uk/pdbsum/4o1l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4o1l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 04:43, 27 January 2015

OCA — Tue, 27 Jan 2015 04:43:39 GMT

←Older revision		Revision as of 04:43, 27 January 2015
Line 20:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+
		+	==See Also==
		+	*[[Adenosine kinase\|Adenosine kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:53, 26 November 2014

OCA — Wed, 26 Nov 2014 07:53:19 GMT

←Older revision		Revision as of 07:53, 26 November 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Human Adenosine Kinase in complex with inhibitor==
		+	<StructureSection load='4o1l' size='340' side='right' caption='[[4o1l]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4o1l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1L FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HO4:5-ETHYNYL-7-(BETA-D-RIBOFURANOSYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>HO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pvv\|4pvv]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </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=4o1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o1l RCSB], [http://www.ebi.ac.uk/pdbsum/4o1l PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN]] Defects in ADK are the cause of hypermethioninemia due to adenosine kinase deficiency (HMAKD) [MIM:[http://omim.org/entry/614300 614300]]. A metabolic disorder characterized by global developmental delay, early-onset seizures, mild dysmorphic features, and characteristic biochemical anomalies, including persistent hypermethioninemia with increased levels of S-adenosylmethionine and S-adenosylhomocysteine. Homocysteine levels are typically normal.<ref>PMID:21963049</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ADK_HUMAN ADK_HUMAN]] ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Adenosine kinase (ADK) from Mycobacterium tuberculosis (Mtb) was selected as a target for design of antimycobacterial nucleosides. Screening of 7-(het)aryl-7-deazaadenine ribonucleosides with Mtb and human (h) ADKs and testing with wild-type and drug-resistant Mtb strains identified specific inhibitors of Mtb ADK with micromolar antimycobacterial activity and low cytotoxicity. X-ray structures of complexes of Mtb and hADKs with 7-ethynyl-7-deazaadenosine showed differences in inhibitor interactions in the adenosine binding sites. 1D (1)H STD NMR experiments revealed that these inhibitors are readily accommodated into the ATP and adenosine binding sites of Mtb ADK, whereas they bind preferentially into the adenosine site of hADK. Occupation of the Mtb ADK ATP site with inhibitors and formation of catalytically less competent semiopen conformation of MtbADK after inhibitor binding in the adenosine site explain the lack of phosphorylation of 7-substituted-7-deazaadenosines. Semiempirical quantum mechanical analysis confirmed different affinity of nucleosides for the Mtb ADK adenosine and ATP sites.

-	~~The entry 4o1l is ON HOLD until Paper Publication~~	+	Structural Basis for Inhibition of Mycobacterial and Human Adenosine Kinase by 7-Substituted 7-(Het)aryl-7-deazaadenine Ribonucleosides.,Snasel J, Naus P, Dostal J, Hnizda A, Fanfrlik J, Brynda J, Bourderioux A, Dusek M, Dvorakova H, Stolarikova J, Zabranska H, Pohl R, Konecny P, Dzubak P, Votruba I, Hajduch M, Rezacova P, Veverka V, Hocek M, Pichova I J Med Chem. 2014 Oct 23;57(20):8268-79. doi: 10.1021/jm500497v. Epub 2014 Oct 8. PMID:25259627<ref>PMID:25259627</ref>

-	~~Authors~~: Brynda, J., Dostal, J., Pichova, I~~., Hodcek, M.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Human Adenosine Kinase in~~ complex ~~with inhibitor~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Adenosine kinase]]
		+	[[Category: Brynda, J]]
		+	[[Category: Dostal, J]]
		+	[[Category: Hodcek, M]]
		+	[[Category: Pichova, I]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 07:23, 5 November 2014

OCA — Wed, 05 Nov 2014 07:23:47 GMT

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-	The entry 4o1l is ON HOLD	+	The entry 4o1l is ON HOLD until Paper Publication

	Authors: Brynda, J., Dostal, J., Pichova, I., Hodcek, M.		Authors: Brynda, J., Dostal, J., Pichova, I., Hodcek, M.

	Description: Human Adenosine Kinase in complex with inhibitor		Description: Human Adenosine Kinase in complex with inhibitor

OCA at 08:23, 2 April 2014

OCA — Wed, 02 Apr 2014 08:23:10 GMT

←Older revision		Revision as of 08:23, 2 April 2014
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	The entry 4o1l is ON HOLD		The entry 4o1l is ON HOLD

-	Authors: Brynda J., Dostal J., Pichova I., Hodcek M.	+	Authors: Brynda, J., Dostal, J., Pichova, I., Hodcek, M.

	Description: Human Adenosine Kinase in complex with inhibitor		Description: Human Adenosine Kinase in complex with inhibitor

OCA: Protected "4o1l" [edit=sysop:move=sysop]

OCA — Wed, 25 Dec 2013 09:30:24 GMT

Protected "4o1l" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:30, 25 December 2013

OCA: New page: '''Unreleased structure''' The entry 4o1l is ON HOLD Authors: Brynda J., Dostal J., Pichova I., Hodcek M. Description: Human Adenosine Kinase in complex with inhibitor

OCA — Wed, 25 Dec 2013 09:30:24 GMT

New page: '''Unreleased structure''' The entry 4o1l is ON HOLD Authors: Brynda J., Dostal J., Pichova I., Hodcek M. Description: Human Adenosine Kinase in complex with inhibitor

New page

'''Unreleased structure'''

The entry 4o1l is ON HOLD

Authors: Brynda J., Dostal J., Pichova I., Hodcek M.

Description: Human Adenosine Kinase in complex with inhibitor