4bh9
From Proteopedia
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| - | + | ==A structural model of CAP mutant (T127L and S128I) in the apo state== | |
| - | + | <StructureSection load='4bh9' size='340' side='right' caption='[[4bh9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4bh9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BH9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bhp|4bhp]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4bh9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers several advantages over competitive inhibition, but the mechanisms of action remain poorly understood in most cases. Here we show that allosteric inhibition can be effected by destabilizing a low-populated conformational state that serves as an on-pathway intermediate for ligand binding, without altering the protein's ground-state structure. As standard structural approaches are typically concerned with changes in the ground-state structure of proteins, the presence of such a mechanism can go easily undetected. Our data strongly argue for the routine use of NMR tools suited to detect and characterize transiently formed conformational states in allosteric systems. Structure information on such important intermediates can ultimately result in more efficient design of allosteric inhibitors. | ||
| - | + | Allosteric inhibition through suppression of transient conformational states.,Tzeng SR, Kalodimos CG Nat Chem Biol. 2013 May 5. doi: 10.1038/nchembio.1250. PMID:23644478<ref>PMID:23644478</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Catabolite gene activator protein|Catabolite gene activator protein]] | |
| - | [[Category: | + | == References == |
| - | [[Category: Kalodimos, C G | + | <references/> |
| - | [[Category: Tzeng, S R | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Kalodimos, C G]] | ||
| + | [[Category: Tzeng, S R]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 10:02, 21 December 2014
A structural model of CAP mutant (T127L and S128I) in the apo state
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