Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters

Oliver H Weiergräber; Andreas Eckhoff; Joachim Granzin

doi:10.1016/j.febslet.2005.12.007

Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters

FEBS Lett. 2006 Jan 9;580(1):251-5. doi: 10.1016/j.febslet.2005.12.007. Epub 2005 Dec 12.

Authors

Oliver H Weiergräber¹, Andreas Eckhoff, Joachim Granzin

Affiliation

¹ Institut für Biologische Informationsverarbeitung, IBI-2, Biologische Strukturforschung, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany.

PMID: 16364310
DOI: 10.1016/j.febslet.2005.12.007

Abstract

We present the three-dimensional structure of the N-terminal FK506-binding protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana. The data provide the structural background for the explanation of key functional properties reported previously.

MeSH terms

ATP Binding Cassette Transporter, Subfamily B / metabolism
Arabidopsis / chemistry*
Arabidopsis / metabolism
Arabidopsis Proteins / chemistry*
Arabidopsis Proteins / metabolism
Protein Structure, Tertiary
Structure-Activity Relationship
Tacrolimus Binding Proteins / chemistry*
Tacrolimus Binding Proteins / metabolism

Substances

ATP Binding Cassette Transporter, Subfamily B
Arabidopsis Proteins
TWD1 protein, Arabidopsis
Tacrolimus Binding Proteins