4bhp | pdb_00004bhp

A structural model of CAP mutant (T127L and S128I) in cGMP-bound state

spinqualitylabelsall models 4bhp, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bhp is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4bh9 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catabolite gene activator protein

Proteopedia Page Contributors and Editors (what is this?)

OCA