3WH0

Structure of Pin1 Complex with 18-crown-6

Summary for 3WH0

• Entry DOI: 10.2210/pdb3wh0/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, SULFATE ION, 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE, ... (5 entities in total)
• Functional Keywords: isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13526
• Total number of polymer chains: 1
• Total formula weight: 18964.14

Authors

Lee, C.C.,Liu, C.I.,Jeng, W.Y.,Wang, A.H.J. (deposition date: 2013-08-20, release date: 2014-10-15, Last modification date: 2024-05-29)

Primary citation

Lee, C.C.,Maestre-Reyna, M.,Hsu, K.C.,Wang, H.C.,Liu, C.I.,Jeng, W.Y.,Lin, L.L.,Wood, R.,Chou, C.C.,Yang, J.M.,Wang, A.H.
Crowning proteins: modulating the protein surface properties using crown ethers.
Angew.Chem.Int.Ed.Engl., 53:13054-13058, 2014

PubMed Abstract: 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.

PubMed: 25287606
DOI: 10.1002/anie.201405664

Experimental method

X-RAY DIFFRACTION (1.6 Å)