5nor: Difference between revisions
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==Structure of cyclophilin A in complex with 3-methylpyridin-2-amine== | ==Structure of cyclophilin A in complex with 3-methylpyridin-2-amine== | ||
<StructureSection load='5nor' size='340' side='right' caption='[[5nor]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5nor' size='340' side='right'caption='[[5nor]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nor]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOR OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5nor]] 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=5NOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NOR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=93Q:3-methylpyridin-2-amine'>93Q</scene></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=5nor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nor OCA], [https://pdbe.org/5nor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nor RCSB], [https://www.ebi.ac.uk/pdbsum/5nor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nor ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5nor" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5nor" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Georgiou | [[Category: Large Structures]] | ||
[[Category: Ioannidis | [[Category: Georgiou C]] | ||
[[Category: Julien | [[Category: Ioannidis H]] | ||
[[Category: Mcnae | [[Category: Julien M]] | ||
[[Category: Walkinshaw | [[Category: Mcnae IW]] | ||
[[Category: Walkinshaw MD]] | |||
Latest revision as of 16:16, 15 November 2023
Structure of cyclophilin A in complex with 3-methylpyridin-2-amineStructure of cyclophilin A in complex with 3-methylpyridin-2-amine
Structural highlights
FunctionPPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Publication Abstract from PubMedFragment-based drug discovery is an increasingly popular method to identify novel small-molecule drug candidates. One of the limitations of the approach is the difficulty of accurately characterizing weak binding events. This work reports a combination of X-ray diffraction, surface plasmon resonance experiments and molecular dynamics simulations for the characterization of binders to different isoforms of the cyclophilin (Cyp) protein family. Although several Cyp inhibitors have been reported in the literature, it has proven challenging to achieve high binding selectivity for different isoforms of this protein family. The present studies have led to the identification of several structurally novel fragments that bind to diverse Cyp isoforms in distinct pockets with low millimolar dissociation constants. A detailed comparison of the merits and drawbacks of the experimental and computational techniques is presented, and emerging strategies for designing ligands with enhanced isoform specificity are described. Pushing the Limits of Detection of Weak Binding Using Fragment-Based Drug Discovery: Identification of New Cyclophilin Binders.,Georgiou C, McNae I, Wear M, Ioannidis H, Michel J, Walkinshaw M J Mol Biol. 2017 Aug 4;429(16):2556-2570. doi: 10.1016/j.jmb.2017.06.016. Epub, 2017 Jun 30. PMID:28673552[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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