4flj

From Proteopedia

(Difference between revisions)

Revision as of 19:56, 19 October 2022

Human MetAP1 with bengamide analog Y08, in Mn form

Structural highlights

4flj 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.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] ^[2]

Publication Abstract from PubMed

Natural-product-derived bengamides possess potent antiproliferative activity and target human methionine aminopeptidases (MetAPs) for their cellular effects. Several derivatives were designed, synthesized, and evaluated as MetAP inhibitors. Here, we present four new X-ray structures of human MetAP1 in complex with the inhibitors. Together with the previous structures of bengamide derivatives with human MetAP2 and tubercular MtMetAP1c, analysis of the interactions of these inhibitors at the active site provides structural basis for further modification of these bengamide inhibitors for improved potency and selectivity as anticancer and antibacterial therapeutics.

Structural Analysis of Bengamide Derivatives as Inhibitors of Methionine Aminopeptidases.,Xu W, Lu JP, Ye QZ J Med Chem. 2012 Sep 14. PMID:22913487^[3]

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

References

↑ Addlagatta A, Hu X, Liu JO, Matthews BW. Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:16274222 doi:10.1021/bi051691k
↑ Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18148-53. Epub 2006 Nov 17. PMID:17114291
↑ Xu W, Lu JP, Ye QZ. Structural Analysis of Bengamide Derivatives as Inhibitors of Methionine Aminopeptidases. J Med Chem. 2012 Sep 14. PMID:22913487 doi:http://dx.doi.org/10.1021/jm3008695

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4flj"

Categories: Homo sapiens | Large Structures | Xu W | Ye QZ

@@ Line 1: / Line 1: @@
 ==Human MetAP1 with bengamide analog Y08, in Mn form==
-<StructureSection load='4flj' size='340' side='right' caption='[[4flj]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
+<StructureSection load='4flj' size='340' side='right'caption='[[4flj]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4flj]] 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=4FLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FLJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4flj]] 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=4FLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FLJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=Y08:(E,2R,3R,4S,5R)-N-[[(3S)-1-CYCLOPROPYLCARBONYLPIPERIDIN-3-YL]METHYL]-2-METHOXY-8,8-DIMETHYL-3,4,5-TRIS(OXIDANYL)NON-6-ENAMIDE'>Y08</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=Y08:(E,2R,3R,4S,5R)-N-[[(3S)-1-CYCLOPROPYLCARBONYLPIPERIDIN-3-YL]METHYL]-2-METHOXY-8,8-DIMETHYL-3,4,5-TRIS(OXIDANYL)NON-6-ENAMIDE'>Y08</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pka|3pka]], [[3pkb|3pkb]], [[3pkc|3pkc]], [[3pkd|3pkd]], [[3pke|3pke]], [[4fli|4fli]], [[4flk|4flk]], [[4fll|4fll]]</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=4flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4flj OCA], [https://pdbe.org/4flj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4flj RCSB], [https://www.ebi.ac.uk/pdbsum/4flj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4flj ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0094, map1, METAP1 ([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=4flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4flj OCA], [http://pdbe.org/4flj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4flj RCSB], [http://www.ebi.ac.uk/pdbsum/4flj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4flj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AMPM1_HUMAN AMPM1_HUMAN]] Removes the N-terminal methionine from nascent proteins. Required for normal progression through the cell cycle.<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 ==
@@ Line 21: / Line 18: @@
 </div>
 <div class="pdbe-citations 4flj" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Methionyl aminopeptidase]]
+[[Category: Large Structures]]
-[[Category: Xu, W]]
+[[Category: Xu W]]
-[[Category: Ye, Q Z]]
+[[Category: Ye QZ]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]

4flj

From Proteopedia

Revision as of 19:56, 19 October 2022

Human MetAP1 with bengamide analog Y08, in Mn form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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