3t8v
From Proteopedia
(Difference between revisions)
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==A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases== | ==A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases== | ||
| - | <StructureSection load='3t8v' size='340' side='right' caption='[[3t8v]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3t8v' size='340' side='right'caption='[[3t8v]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3t8v]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3t8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafq Plafq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T8V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTJ:N-[(2-{2-[(N-{(2S,3R)-3-AMINO-4-[4-(BENZYLOXY)PHENYL]-2-HYDROXYBUTANOYL}-L-ALANYL)AMINO]ETHOXY}ETHOXY)ACETYL]-4-BENZOYL-L-PHENYLALANYL-N~6~-HEX-5-YNOYLLYSINAMIDE'>BTJ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTJ:N-[(2-{2-[(N-{(2S,3R)-3-AMINO-4-[4-(BENZYLOXY)PHENYL]-2-HYDROXYBUTANOYL}-L-ALANYL)AMINO]ETHOXY}ETHOXY)ACETYL]-4-BENZOYL-L-PHENYLALANYL-N~6~-HEX-5-YNOYLLYSINAMIDE'>BTJ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ebg|3ebg]], [[3t8w|3t8w]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ebg|3ebg]], [[3t8w|3t8w]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t8v OCA], [https://pdbe.org/3t8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t8v RCSB], [https://www.ebi.ac.uk/pdbsum/3t8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t8v ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/AMP1_PLAFQ AMP1_PLAFQ]] Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.<ref>PMID:12166515</ref> <ref>PMID:19196988</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
| - | *[[Aminopeptidase|Aminopeptidase]] | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Plafq]] | [[Category: Plafq]] | ||
[[Category: Greebaum, D C]] | [[Category: Greebaum, D C]] | ||
Revision as of 16:47, 6 July 2022
A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases
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