Aromatic–aromatic interactions in proteins: beyond the dimer
2011, Journal of chemical information and modeling 51 (7), 1623-1633, 2011Citas: 138
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Autor(es)
Esteban Lanzarotti and Rolf R Biekofsky and Darío A Estrin and Marcelo A Marti and Adrián G Turjanski
URL Pública
https://pubs.acs.org/doi/abs/10.1021/ci200062eAbstract
Aromatic residues are key widespread elements of protein structures and have been shown to be important for structure stability, folding, protein–protein recognition, and ligand binding. The interactions of pairs of aromatic residues (aromatic dimers) have been extensively studied in protein structures. Isolated aromatic molecules tend to form higher order clusters, like trimers, tetramers, and pentamers, that adopt particular well-defined structures. Taking this into account, we have surveyed protein structures deposited in the Protein Data Bank in order to find clusters of aromatic residues in proteins larger than dimers and characterized them. Our results show that larger clusters are found in one of every two unique proteins crystallized so far, that the clusters are built adopting the same trimer motifs found for benzene clusters in vacuum, and that they are clearly nonlocal brining primary structure distant sites together …
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