3wur | pdb_00003wur

Structure of DMP19 Complex with 18-crown-6

spinqualitylabelsall models 3wur, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wur is a 2 chain structure with sequence from Neisseria meningitidis MC58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: EDO, O4B, SO4, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9K0P4_NEIMB Publication Abstract from PubMed Crown 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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