Structural highlights
Function
HMEN_DROME This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
Publication Abstract from PubMed
Water molecules can interact with aromatic moieties using either their O-H bonds or their lone-pairs of electrons. In proteins, water-pi interactions have been reported to occur with tryptophan and histidine residues, and dynamic exchange between O-Hpi hydrogen bonding and lone-pairpi interactions was suggested to take place, based on ab initio calculations. Here we used classical and QM/MM molecular dynamics simulations, complemented with an NMR study, to examine a specific water-indole interaction observed in the engrailed homeodomain and in its mutants. Our simulations indicate that the binding mode between water and indole can adapt to the potential created by the surrounding amino acids (and by the residues at the DNA surface in protein-DNA complexes), and support the model of dynamic switching between the O-Hpi hydrogen bonding and lone-pairpi binding modes.
Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants.,Spackova N, Trosanova Z, Sebesta F, Jansen S, Burda JV, Srb P, Zachrdla M, Zidek L, Kozelka J Phys Chem Chem Phys. 2018 May 9;20(18):12664-12677. doi: 10.1039/c7cp08623g. PMID:29696277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Špačková N, Trošanová Z, Šebesta F, Jansen S, Burda JV, Srb P, Zachrdla M, Žídek L, Kozelka J. Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants. Phys Chem Chem Phys. 2018 May 9;20(18):12664-12677. PMID:29696277 doi:10.1039/c7cp08623g
