5knh: Difference between revisions
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<StructureSection load='5knh' size='340' side='right'caption='[[5knh]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5knh' size='340' side='right'caption='[[5knh]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5knh]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5knh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_fascicularis Macaca fascicularis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KNH 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]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=5knh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5knh OCA], [https://pdbe.org/5knh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5knh RCSB], [https://www.ebi.ac.uk/pdbsum/5knh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5knh 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/Q0PW92_MACFA Q0PW92_MACFA] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synthetic construct | [[Category: Macaca fascicularis]] | ||
[[Category: Gilliland | [[Category: Synthetic construct]] | ||
[[Category: Malia | [[Category: Gilliland G]] | ||
[[Category: Obmolova | [[Category: Malia T]] | ||
[[Category: Teplyakov | [[Category: Obmolova G]] | ||
[[Category: Teplyakov A]] | |||
Latest revision as of 13:04, 27 September 2023
CRYSTAL STRUCTURE OF DARPIN 6G9 IN COMPLEX WITH CYNO IL-13CRYSTAL STRUCTURE OF DARPIN 6G9 IN COMPLEX WITH CYNO IL-13
Structural highlights
FunctionPublication Abstract from PubMedDesigned ankyrin repeat proteins (DARPin(R)) are artificial non-immunoglobulin binding proteins with potential applications as therapeutic molecules. DARPin 6G9 binds interleukin-13 with high affinity and blocks the signaling pathway and as such is promising for the treatment of asthma and other atopic diseases. The crystal structures of DARPin 6G9 in the unbound form and in complex with IL-13 were determined at high resolution. The DARPin competes for the same epitope as the IL-13 receptor chain 13Ralpha1 but does not interfere with the binding of the other receptor chain, IL-4Ralpha. Analysis of multiple copies of the DARPin molecule in the crystal indicates the conformational instability in the N-terminal cap that was predicted from molecular dynamics simulations. Comparison of the DARPin structures in the free state and in complex with IL-13 reveals a concerted movement of the ankyrin repeats upon binding resulted in the opening of the binding site. The induced-fit mode of binding employed by DARPin 6G9 is very unusual for DARPins since they were designed as particularly stable and rigid molecules. This finding shows that DARPins can operate by various binding mechanisms and suggests that some flexibility in the scaffold may be an advantage. Conformational flexibility of an anti-IL-13 DARPindagger.,Teplyakov A, Malia TJ, Obmolova G, Jacobs SA, O'Neil KT, Gilliland GL Protein Eng Des Sel. 2016 Nov 23. PMID:27881684[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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