Determination of Dipeptide Ligand Binding Affinity to Cyp3 by Crystal Soaking Method
Amir Rabu, and Wear, Martin A., and Walkinshaw, Malcolm D., (2007) Determination of Dipeptide Ligand Binding Affinity to Cyp3 by Crystal Soaking Method. Malaysian Journal of Biochemistry and Molecular Biology, 15 (2). pp. 72-75. ISSN ISSN 1511-2616 Full text not available from this repository. Official URL: http://ejum.fsktm.um.edu.my/ArticleInformation.aspx?ArticleID=571 AffiliationsUniversiti Kebangsaan Malaysia. Faculty of Science and Technology. School of Biosciences and Biotechnology
University of Edinburgh. Institute of Structural and Molecular Biology
University of Edinburgh. Institute of Structural and Molecular Biology AbstractCrystal soaking is one of the techniques used in X-ray crystallography to obtain a 3D structure of protein complex with certain ligands. In addition, the technique has been widely used in crystal phasing. The work described here outlines a novel method of studying ligand-protein interactions by using X-ray protein crystallography. In this study, the dissociation constant of the ligand in the crystal (Kdc), which indicates the affinity of the interaction, was calculated by SHELX97 program. This is based on the occupancy of ligands at the binding pocket; obtained by soaking the crystals in increasing concentrations of ligand. Cyclophilin 3 (Cyp3) protein crystals were used as a model to study its interaction with dipeptide Gly-Pro by soaking them in increasing concentrations of dipeptide up to 150 mM. Results showed that the crystal dissociation constant (Kdc) of Gly-Pro-Cyp3 complex is 37.6 μM, which is almost similar to its solution dissociation constant (Kds) obtained by PPIase assay. Repository Staff Only: item control page
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