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  • Title: Aromatic side-chain interactions in proteins. Near- and far-sequence His-X pairs.
    Author: Meurisse R, Brasseur R, Thomas A.
    Journal: Biochim Biophys Acta; 2003 Jun 26; 1649(1):85-96. PubMed ID: 12818194.
    Abstract:
    Several studies have analysed aromatic interactions, involving mostly phenylalanine, tyrosine and tryptophan. Only a few studies have considered histidine as an interacting aromatic residue. An extensive analysis of aromatic His-X interactions is performed here on a data set of 593 PDB structures: 68% of the histidine are involved in aromatic pairs and 1271 non-redundant His-X pairs were analysed. Thirty percent of these pairs involve an aromatic partner less than 6 apart in the sequence. These near-sequence pairs correspond to conformations which stabilise secondary structures, mainly alpha-helices when the residues are 4 apart and beta-strands when they are 2 apart in the sequence. The partners of the other His-X pairs (887, 70%) are more than 5 apart in the sequence. Of these far-sequence pairs, 35% bridge beta strands and only 9% helices. The near-sequence pairs are sterically constrained as supported by conformer distribution. The X partners of far-sequence His-X pairs are mainly "above" the histidine ring with tilted and normal rings, corresponding to a "T shape; face to edge" orientation. Phenylalanine, the only aromatic residue with no heteroatom, is a disfavoured partner, whereas histidine is the preferred one. Heteroatom-heteroatom interactions are favoured in near-sequence as well as in far-sequence His-His, His-Trp and His-Tyr pairs.
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