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Conformational flexibility and ligand binding properties of ovine Beta-lactoglobulin

100%

Loch J. I., Bonarek P., Lewinski K.

Acta Biochimica Polonica

2019

tom 66

nr 4

Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket

88%

Loch J. I., Bonarek P., Siuda M., Wrobel P., Lewinski K.

Acta Biochimica Polonica

2021

tom 68

nr 1

Prostatic acid phosphatase: structural aspects of inhibition by L-[plus]-tartrate ions

76%

Lovelace L., Lewinski K., Jakob C. G., Kuciel R., Ostrowski W., Lebioda L.

Acta Biochimica Polonica

1997

tom 44

nr 4

The crystal structure of the complex between rat-prostatic acid phosphatase (PAP) and L-(+)-tartrate (Lindqvist et al., J. Biol. Chem., 1993, 268, 20744-20746) contains the model of the ligand with incorrect chirality. We report here the correct model and discuss the relation between this model and the model of the inhibitory complexes between PAP and oxy-anions.

Ograniczanie wyników

3 Acta Biochimica Polonica

3 Lewinski K.

2 Bonarek P.

2 Loch J. I.

1 Jakob C. G.

1 Kuciel R.

1 Lebioda L.

1 Lovelace L.

1 Ostrowski W.

1 Siuda M.

1 Wrobel P.

1 2021

1 2019

1 1997

Wyniki wyszukiwania

Conformational flexibility and ligand binding properties of ovine Beta-lactoglobulin

Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket

Prostatic acid phosphatase: structural aspects of inhibition by L-[plus]-tartrate ions