4BHP
A structural model of CAP mutant (T127L and S128I) in cGMP-bound state
Summary for 4BHP
| Entry DOI | 10.2210/pdb4bhp/pdb |
| Related | 4BH9 |
| NMR Information | BMRB: 19145 |
| Descriptor | CAMP RECEPTOR PROTEIN (1 entity in total) |
| Functional Keywords | transcription |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 23579.38 |
| Authors | Tzeng, S.R.,Kalodimos, C.G. (deposition date: 2013-04-04, release date: 2013-05-08, Last modification date: 2024-06-19) |
| Primary citation | Tzeng, S.R.,Kalodimos, C.G. Allosteric Inhibition Through Suppression of Transient Conformational States. Nat.Chem.Biol., 9:462-, 2013 Cited by PubMed Abstract: 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. PubMed: 23644478DOI: 10.1038/NCHEMBIO.1250 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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