4z2h: Difference between revisions
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==Serratia marcescens Chitinase B complexed with macrolide inhibitor 29== | ==Serratia marcescens Chitinase B complexed with macrolide inhibitor 29== | ||
<StructureSection load='4z2h' size='340' side='right' caption='[[4z2h]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4z2h' size='340' side='right'caption='[[4z2h]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z2h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z2H OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4z2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z2H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M6A:(1R,2R,3R,6R,7S,8S,9R,10R,12R,13S,17S)-3-ETHYL-2,10-DIHYDROXY-2,6,8,10,12,15,15,17-OCTAMETHYL-5-OXO-9-(PROP-2-YN-1-YLOXY)-4,14,16-TRIOXABICYCLO[11.3.1]HEPTADEC-7-YL+{2-[N-(METHYLCARBAMOYL)CARBAMIMIDAMIDO]ETHYL}CARBAMATE'>M6A</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M6A:(1R,2R,3R,6R,7S,8S,9R,10R,12R,13S,17S)-3-ETHYL-2,10-DIHYDROXY-2,6,8,10,12,15,15,17-OCTAMETHYL-5-OXO-9-(PROP-2-YN-1-YLOXY)-4,14,16-TRIOXABICYCLO[11.3.1]HEPTADEC-7-YL+{2-[N-(METHYLCARBAMOYL)CARBAMIMIDAMIDO]ETHYL}CARBAMATE'>M6A</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=4z2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z2h OCA], [https://pdbe.org/4z2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z2h RCSB], [https://www.ebi.ac.uk/pdbsum/4z2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z2h ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CHIB_SERMA CHIB_SERMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Chitinase|Chitinase]] | *[[Chitinase 3D structures|Chitinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Serratia marcescens]] | ||
[[Category: | [[Category: Maita N]] | ||
[[Category: | [[Category: Sugawara A]] | ||
[[Category: | [[Category: Sunazuka T]] | ||
Latest revision as of 18:41, 8 November 2023
Serratia marcescens Chitinase B complexed with macrolide inhibitor 29Serratia marcescens Chitinase B complexed with macrolide inhibitor 29
Structural highlights
FunctionPublication Abstract from PubMedArgifin, a 17-membered pentapeptide, inhibits chitinase. As argifin has properties that render it unsuitable as a drug development candidate, we devised a mechanism to create the structural component of argifin that bestows the chitinase inhibition and introduce it into a 14-membered macrolide scaffold. Here we describe (1) the designed macrolide, which exhibits approximately 200-fold more potent chitinase inhibition than argifin, (2) the binding modes of the macrolide with Serratia marcescens chitinase B, and (3) the computed analysis explaining the reason for derivatives displaying increased inhibition compared to argifin, the macrolide aglycone displaying inhibition in a nanomolar range. This promises a class of chitinase inhibitors with novel skeletons, providing innovative insight for drug design and the use of macrolides as adaptable, flexible templates for use in drug discovery research and development. Creation of Customized Bioactivity within a 14-Membered Macrolide Scaffold: Design, Synthesis, and Biological Evaluation Using a Family-18 Chitinase.,Sugawara A, Maita N, Gouda H, Yamamoto T, Hirose T, Kimura S, Saito Y, Nakano H, Kasai T, Nakano H, Shiomi K, Hirono S, Watanabe T, Taniguchi H, Omura S, Sunazuka T J Med Chem. 2015 Jun 25;58(12):4984-4997. Epub 2015 Jun 12. PMID:26030312[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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