8oh7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of A4M4C bound to (KR)4 Solution backbone structure refined by PCS== | |
| + | <StructureSection load='8oh7' size='340' side='right'caption='[[8oh7]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8oh7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OH7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8oh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oh7 OCA], [https://pdbe.org/8oh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oh7 RCSB], [https://www.ebi.ac.uk/pdbsum/8oh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oh7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ultra-tight binding is usually observed for proteins associating with rigidified molecules. Previously, we demonstrated that femtomolar binders derived from the Armadillo repeat proteins (ArmRPs) can be designed to interact very tightly with fully flexible peptides. Here we show for ArmRPs with four and seven sequence-identical internal repeats that the peptide-ArmRP complexes display conformational dynamics. These dynamics stem from transient breakages of individual protein-residue contacts that are unrelated to overall unbinding. The labile contacts involve electrostatic interactions. We speculate that these dynamics allow attaining very high binding affinities, since they reduce entropic losses. Importantly, only NMR techniques can pick up these local events by directly detecting conformational exchange processes without complications from changes in solvent entropy. Furthermore, we demonstrate that the interaction surface of the repeat protein regularizes upon peptide binding to become more compatible with the peptide geometry. These results provide novel design principles for ultra-tight binders. | ||
| - | + | Unexpected dynamics in femtomolar complexes of binding proteins with peptides.,Cucuzza S, Sitnik M, Jurt S, Michel E, Dai W, Muntener T, Ernst P, Haussinger D, Pluckthun A, Zerbe O Nat Commun. 2023 Nov 28;14(1):7823. doi: 10.1038/s41467-023-43596-2. PMID:38016954<ref>PMID:38016954</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8oh7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cucuzza S]] | ||
| + | [[Category: Zerbe O]] | ||
Current revision
Structure of A4M4C bound to (KR)4 Solution backbone structure refined by PCS
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