2014
DOI: 10.1002/prot.24639
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Molecular dynamics simulations of the auxin-binding protein 1 in complex with indole-3-acetic acid and naphthalen-1-acetic acid

Abstract: Auxin-binding protein 1 (ABP1) is suggested to be an auxin receptor which plays an important role in several processes in green plants. Maize ABP1 was simulated with the natural auxin indole-3-acetic acid (IAA) and the synthetic analog naphthalen-1-acetic acid (NAA), to elucidate the role of the KDEL sequence and the helix at the C-terminus. The KDEL sequence weakens the intermolecular interactions between the monomers but stabilizes the C-terminal helix. Conformational changes at the C-terminus occur within t… Show more

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Cited by 4 publications
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“…Since structural differences of the majority of compounds displayed in Table 3 are related to the 3-side chain, variations in their binding affinities mostly reflect the differences in the binding capacities of their polar groups to the receptor site. A recent molecular dynamic simulation study [ 42 ] has shown that the interaction between the carboxyl group of IAA and the zinc ion of the binding site was very strong. It seems reasonable to assume that the rest of the indole-3-carboxylic acids also form favorable interactions with the Zn ion.…”
Section: Resultsmentioning
confidence: 99%
“…Since structural differences of the majority of compounds displayed in Table 3 are related to the 3-side chain, variations in their binding affinities mostly reflect the differences in the binding capacities of their polar groups to the receptor site. A recent molecular dynamic simulation study [ 42 ] has shown that the interaction between the carboxyl group of IAA and the zinc ion of the binding site was very strong. It seems reasonable to assume that the rest of the indole-3-carboxylic acids also form favorable interactions with the Zn ion.…”
Section: Resultsmentioning
confidence: 99%