3WHM
Structure of Hemoglobin Complex with 18-crown-6
Summary for 3WHM
| Entry DOI | 10.2210/pdb3whm/pdb |
| Related | 3WH0 |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total) |
| Functional Keywords | 18-crown-6, heme-binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 65964.62 |
| Authors | Lee, C.C.,Lin, L.L.,Wang, A.H.J. (deposition date: 2013-08-27, release date: 2014-10-15, Last modification date: 2023-11-08) |
| 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 Cited by 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: 25287606DOI: 10.1002/anie.201405664 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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