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Molecular recognition of the plant hormone auxin is still a puzzle (CROSBI ID 483064)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Kojić-Prodić, Biserka ; Magnus, Volker ; Tomić, Sanja ; Antolić, Snježana ; Salopek-Sondi, Branka ; Dolušić, Eduard ; Bertoša, Branimir Molecular recognition of the plant hormone auxin is still a puzzle // Abstracts, XIX Congress and General Assembly of the International Union of Crystallography [Acta Crystallographica A58 (Supplement)] / N. N. (ur.). Chester: International Union of Crystallography, 2002. str. C139-C139-x

Podaci o odgovornosti

Kojić-Prodić, Biserka ; Magnus, Volker ; Tomić, Sanja ; Antolić, Snježana ; Salopek-Sondi, Branka ; Dolušić, Eduard ; Bertoša, Branimir

engleski

Molecular recognition of the plant hormone auxin is still a puzzle

The plant hormone auxin is involved in almost every aspect of plant development; auxin homeostasis and auxin signaling are thus of crucial importance. The wider auxin family includes endogenous growth promoters, such as indole-3-acetic acid (IAA), and chemically diverse synthetic analogues; minor structural modifications afford growth inhibitors (antiauxins). As proper classification is of technological relevance (growth regulators, herbicides) we developed a classification by interaction similarity indices, based on the evaluation of two distinctive molecular conformations (planar and tilted) of indole-3-acetic acid in comparison with the optimized conformations of 50 compounds. Then we extended the method to a larger set of compounds using similarity of molecular interaction fields and lipophilicity predictions (log P). In addition to theoretical approaches based on the evaluation of molecular conformations of possible relevance for binding to the auxin receptor(s), we used experimental methods, such as X-ray structure analysis and spectroscopic methods to characterize the molecules of interest: alkylated IAAs, halogenated IAAs (F, Cl, Br), and dihalogenated IAAs. Systematic analysis of physico-chemical and structural properties provided indirect insight into the topology of the substrate-binding site of the, so far hypothetical, common auxin receptor. Our findings are in reasonable accord with the models proposed by previous researchers. The question of molecular fit to the receptor active site will, however, remain open until the coordinates of the first structurally characterized auxin binding protein, ABP1, will be in the public domain.

molecular recognition; auxin

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Podaci o prilogu

C139-C139-x.

2002.

objavljeno

Podaci o matičnoj publikaciji

Abstracts, XIX Congress and General Assembly of the International Union of Crystallography [Acta Crystallographica A58 (Supplement)]

N. N.

Chester: International Union of Crystallography

Podaci o skupu

XIX Congress and General Assembly of the International Union of Crystallography

poster

06.08.2002-15.08.2002

Ženeva, Švicarska

Povezanost rada

Kemija, Biologija