7WBN

PDB structure of RevCC

Summary for 7WBN

• Entry DOI: 10.2210/pdb7wbn/pdb
• NMR Information: BMRB: 36464
• Descriptor: RevCC (1 entity in total)
• Functional Keywords: protein, antiviral protein
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 1
• Total formula weight: 11991.57

Authors

Han, S.,Kim, D.,Kaur, M.,Lim, Y.B.,Barnwal, R.P. (deposition date: 2021-12-17, release date: 2022-10-26, Last modification date: 2024-05-15)

Primary citation

Kim, D.I.,Han, S.H.,Park, H.,Choi, S.,Kaur, M.,Hwang, E.,Han, S.J.,Ryu, J.Y.,Cheong, H.K.,Barnwal, R.P.,Lim, Y.B.
Pseudo-Isolated alpha-Helix Platform for the Recognition of Deep and Narrow Targets.
J.Am.Chem.Soc., 144:15519-15528, 2022

PubMed Abstract: Although interest in stabilized α-helical peptides as next-generation therapeutics for modulating biomolecular interfaces is increasing, peptides have limited functionality and stability due to their small size. In comparison, α-helical ligands based on proteins can make steric clash with targets due to their large size. Here, we report the design of a monomeric pseudo-isolated α-helix (mPIH) system in which proteins behave as if they are peptides. The designed proteins contain α-helix ligands that do not require any covalent chemical modification, do not have frayed ends, and importantly can make sterically favorable interactions similar to isolated peptides. An optimal mPIH showed a more than 100-fold increase in target selectivity, which might be related to the advantages in conformational selection due to the absence of frayed ends. The α-helical ligand in the mPIH displayed high thermal stability well above human body temperature and showed reversible and rapid folding/unfolding transitions. Thus, mPIH can become a promising protein-based platform for developing stabilized α-helix pharmaceuticals.

PubMed: 35972994
DOI: 10.1021/jacs.2c03858

Experimental method

SOLUTION NMR