3wur
From Proteopedia
Structure of DMP19 Complex with 18-crown-6
Structural highlights
FunctionPublication Abstract from PubMedCrown ethers are small, cyclic polyethers that have found wide-spread use in phase-transfer catalysis and, to a certain degree, in protein chemistry. Crown ethers readily bind metallic and organic cations, including positively charged amino acid side chains. We elucidated the crystal structures of several protein-crown ether co-crystals grown in the presence of 18-crown-6. We then employed biophysical methods and molecular dynamics simulations to compare these complexes with the corresponding apoproteins and with similar complexes with ring-shaped low-molecular-weight polyethylene glycols. Our studies show that crown ethers can modify protein surface behavior dramatically by stabilizing either intra- or intermolecular interactions. Consequently, we propose that crown ethers can be used to modulate a wide variety of protein surface behaviors, such as oligomerization, domain-domain interactions, stabilization in organic solvents, and crystallization. Crowning Proteins: Modulating the Protein Surface Properties using Crown Ethers.,Lee CC, Maestre-Reyna M, Hsu KC, Wang HC, Liu CI, Jeng WY, Lin LL, Wood R, Chou CC, Yang JM, Wang AH Angew Chem Int Ed Engl. 2014 Oct 6. doi: 10.1002/anie.201405664. PMID:25287606[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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