4u6j - Revision history

OCA at 09:01, 20 March 2024

OCA — Wed, 20 Mar 2024 09:01:02 GMT

←Older revision		Revision as of 09:01, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4u6j]] 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=4U6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U6J FirstGlance]. <br>		<table><tr><td colspan='2'>[[4u6j]] 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=4U6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U6J FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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]] 1.56Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [https://pdbe.org/4u6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [https://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j 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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [https://pdbe.org/4u6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [https://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>		[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The methionine aminopeptidase (MetAP) family is responsible for the cleavage of the initiator methionine from newly synthesized proteins. Currently, there are no small molecule inhibitors that show selectivity toward the bacterial MetAPs compared to the human enzyme. In our current study, we have screened 20 alpha-aminophosphonate derivatives and identified a molecule (compound 15) that selectively inhibits the S. pneumonia MetAP in low micromolar range but not the human enzyme. Further bioinformatics, biochemical, and structural analyses suggested that phenylalanine (F309) in the human enzyme and methionine (M205) in the S. pneumonia MetAP at the analogous position render them with different susceptibilities against the identified inhibitor. X-ray crystal structures of various inhibitors in complex with wild type and F309M enzyme further established the molecular basis for the inhibitor selectivity.
-
-	Identification of the Molecular Basis of Inhibitor Selectivity between the Human and Streptococcal Type I Methionine Aminopeptidases.,Arya T, Reddi R, Kishor C, Ganji RJ, Bhukya S, Gumpena R, McGowan S, Drag M, Addlagatta A J Med Chem. 2015 Mar 12;58(5):2350-7. doi: 10.1021/jm501790e. Epub 2015 Feb 27. PMID:25699713<ref>PMID:25699713</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4u6j" style="background-color:#fffaf0;"></div>

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

OCA at 08:05, 22 March 2023

OCA — Wed, 22 Mar 2023 08:05:20 GMT

←Older revision		Revision as of 08:05, 22 March 2023
Line 3:		Line 3:
	<StructureSection load='4u6j' size='340' side='right'caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>		<StructureSection load='4u6j' size='340' side='right'caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4u6j]] 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=4U6J OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4U6J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4u6j]] 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=4U6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U6J FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [https://pdbe.org/4u6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [https://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METAP1, KIAA0094 ([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/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [~~http~~://pdbe.org/4u6j PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN]] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>	+	[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Methionyl aminopeptidase]]~~	+	[[Category: Addlagatta A]]
-	[[Category: Addlagatta, A]]	+	[[Category: Arya T]]
-	[[Category: Arya, T]]	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 15:03, 10 May 2019

OCA — Fri, 10 May 2019 15:03:52 GMT

←Older revision		Revision as of 15:03, 10 May 2019
Line 1:		Line 1:

	==HsMetAP in complex with methionine==		==HsMetAP in complex with methionine==
-	<StructureSection load='4u6j' size='340' side='right' caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>	+	<StructureSection load='4u6j' size='340' side='right'caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4u6j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4u6j]] 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=4U6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6J FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METAP1, KIAA0094 ([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/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [http://pdbe.org/4u6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [http://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j 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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [http://pdbe.org/4u6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [http://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4u6j" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4u6j" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
	[[Category: Addlagatta, A]]		[[Category: Addlagatta, A]]
	[[Category: Arya, T]]		[[Category: Arya, T]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 01:20, 19 January 2017

OCA — Thu, 19 Jan 2017 01:20:18 GMT

←Older revision		Revision as of 01:20, 19 January 2017
Line 1:		Line 1:
		+
	==HsMetAP in complex with methionine==		==HsMetAP in complex with methionine==
	<StructureSection load='4u6j' size='340' side='right' caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>		<StructureSection load='4u6j' size='340' side='right' caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [http://www.ebi.ac.uk/pdbsum/4u6j 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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [http://pdbe.org/4u6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [http://www.ebi.ac.uk/pdbsum/4u6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4u6j" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:58, 26 March 2015

OCA — Thu, 26 Mar 2015 13:58:56 GMT

←Older revision		Revision as of 13:58, 26 March 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==HsMetAP in complex with methionine==
		+	<StructureSection load='4u6j' size='340' side='right' caption='[[4u6j]], [[Resolution\|resolution]] 1.56Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4u6j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6J FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4u1b\|4u1b]], [[4u69\|4u69]], [[4u6c\|4u6c]], [[4u6e\|4u6e]], [[4u6w\|4u6w]], [[4u6z\|4u6z]], [[4u70\|4u70]], [[4u71\|4u71]], [[4u73\|4u73]], [[4u75\|4u75]], [[4u76\|4u76]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4u6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u6j RCSB], [http://www.ebi.ac.uk/pdbsum/4u6j PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN]] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The methionine aminopeptidase (MetAP) family is responsible for the cleavage of the initiator methionine from newly synthesized proteins. Currently, there are no small molecule inhibitors that show selectivity toward the bacterial MetAPs compared to the human enzyme. In our current study, we have screened 20 alpha-aminophosphonate derivatives and identified a molecule (compound 15) that selectively inhibits the S. pneumonia MetAP in low micromolar range but not the human enzyme. Further bioinformatics, biochemical, and structural analyses suggested that phenylalanine (F309) in the human enzyme and methionine (M205) in the S. pneumonia MetAP at the analogous position render them with different susceptibilities against the identified inhibitor. X-ray crystal structures of various inhibitors in complex with wild type and F309M enzyme further established the molecular basis for the inhibitor selectivity.

-	~~The entry 4u6j is ON HOLD until Paper Publication~~	+	Identification of the Molecular Basis of Inhibitor Selectivity between the Human and Streptococcal Type I Methionine Aminopeptidases.,Arya T, Reddi R, Kishor C, Ganji RJ, Bhukya S, Gumpena R, McGowan S, Drag M, Addlagatta A J Med Chem. 2015 Mar 12;58(5):2350-7. doi: 10.1021/jm501790e. Epub 2015 Feb 27. PMID:25699713<ref>PMID:25699713</ref>

-	~~Authors: Arya~~, T.~~, Addlagatta, A~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~HsMetAP in complex with methionine~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Methionyl aminopeptidase]]
		+	[[Category: Addlagatta, A]]
	[[Category: Arya, T]]		[[Category: Arya, T]]
-	[[Category: ~~Addlagatta, A~~]]	+	[[Category: Hydrolase]]

OCA at 18:11, 24 December 2014

OCA — Wed, 24 Dec 2014 18:11:15 GMT

←Older revision		Revision as of 18:11, 24 December 2014
Line 6:		Line 6:

	Description: HsMetAP in complex with methionine		Description: HsMetAP in complex with methionine
		+	[[Category: Unreleased Structures]]
		+	[[Category: Arya, T]]
		+	[[Category: Addlagatta, A]]

OCA at 06:54, 26 November 2014

OCA — Wed, 26 Nov 2014 06:54:22 GMT

←Older revision		Revision as of 06:54, 26 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4u6j is ON HOLD	+	The entry 4u6j is ON HOLD until Paper Publication

	Authors: Arya, T., Addlagatta, A.		Authors: Arya, T., Addlagatta, A.

	Description: HsMetAP in complex with methionine		Description: HsMetAP in complex with methionine

OCA at 11:40, 19 November 2014

OCA — Wed, 19 Nov 2014 11:40:11 GMT

←Older revision		Revision as of 11:40, 19 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4u6j is ON HOLD ~~until Paper Publication~~	+	The entry 4u6j is ON HOLD

	Authors: Arya, T., Addlagatta, A.		Authors: Arya, T., Addlagatta, A.

	Description: HsMetAP in complex with methionine		Description: HsMetAP in complex with methionine

OCA at 08:05, 13 August 2014

OCA — Wed, 13 Aug 2014 08:05:11 GMT

←Older revision		Revision as of 08:05, 13 August 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4u6j is ON HOLD	+	The entry 4u6j is ON HOLD until Paper Publication

-	Authors: Arya, T, Addlagatta, A	+	Authors: Arya, T., Addlagatta, A.

	Description: HsMetAP in complex with methionine		Description: HsMetAP in complex with methionine

OCA: Protected "4u6j" [edit=sysop:move=sysop]

OCA — Thu, 07 Aug 2014 01:32:00 GMT

Protected "4u6j" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:32, 7 August 2014