In many litratures, I found the allosteric site in TEM-1 is H10 helix , but the explination of how this allosteric site affected by the inhibitors sounds mysterious to me.
Can you please explian these texts for me ?
The presence of an allosteric binding site for TEM- 1 was first recognized by Horn and Shoichet (2004) who showed that the H10 helix moves away from the protein core to allow binding of allosteric inhibitors to a hydrophobic pocket formed by the two helices, H10 and H11 on one side and the b-sheet composed of b3, b4, b5 on the other
Article An evolutionarily conserved allosteric site modulates beta-l...
my questions are :
1- Is H10 helix considered the unique allosteric site that targeted by inhibitors ?
2- If we design drug can target H10 helix in TEM-1 , what exactly will happen to the protein ? how it will help to inhibit the protein ?
3- in the litratures, H11 helix and B3, B4, and B5 mentioned in the allostery of the enzyme, should we target them as well to inhibit the protein ? or targeting H10 helix is enough th modulate the enzyme activity?
Have a look at this paper: Article Allosteric communication in class A β-lactamases occurs via ...
, best on www.ncbi.nlm.nih.gov/pmc/articles/PMC8060031/ to also access the supplementary data. If you 3D superimpose the two structures compared in Figure 1 in a molecule viewer, e.g. PyMOL, you can clearly see how the conformational change of the omega loop induced by allosteric ligand 2 can affect the orthosteric site.- Badges
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