The course objectives are to provide basic knowledge of receptor structure and receptor-ligand interactions and to introduce participants to the fields of molecular biology and structure determination by protein crystallography. The course will take participants from the gene to the three-dimensional crystal structure of a protein.

Cellular communication relies on receptor-ligand interactions. It is therefore essential to gain a detailed structural knowledge of the receptor and the interactions with its ligands. The techniques of molecular biology in combination with X-ray structure determination constitute a strong and efficient tool for the elucidation of the questions concerning the interplay between a ligand or a potential drug and the receptor.

Molecular biological cloning approaches have provided the means to isolate genes and overexpress proteins. Heterologous expression systems are developed to optimise proper folding of the expressed proteins. Methods based on random and directed mutagenesis are instrumental in identifying protein-ligand interactions and in characterising potential domains suitable for crystallisation.

X-ray crystallography is the most powerful experimental method for determining the three-dimensional structures of proteins. Several thousand different protein structures are known today, due to the progress in gene technology, in methods for X-ray data collection and in computer technology. The results have contributed decisively not only to the knowledge of the structure, but also to the knowledge of the biological function of proteins. It is therefore essential for researchers in many different fields within natural science to have a basic knowledge of how to analyse these results and apply them to their own scientific field.

The lectures will cover:

• Introduction to receptors
• Cloning and overexpression of proteins in various species
• Purification of receptor proteins and receptor purity/homogeneity tests
• Biochemical characterisation of receptors
• Crystallisation of receptor proteins
• Protein crystallography
• Structural analysis and databases
• Structure prediction (molecular modelling)
• State of the art 3D receptor structures

The practical exercises will cover:

• Receptor pharmacology
• Biophysical characterization of receptors 
• Crystallisation and data collection of a receptor
• Structural analysis of receptor-ligand complexes
• Search in databases (gene and amino acid sequence, 3D structure etc.)

The course will be organised as a one-week course and will comprise about 18 lectures and 20 hours of practical exercise.

The participants will be supplied with study materials composed of lecture notes or selected scientific publications.

The course will be concluded by a two hour written examination which will be assessed by the course director.

23 to 27 April 2012.

The exam takes place 30 May 2012.

4.5 ECTS credit points (European Credit Transfer System).

110 working hours (30 for preparation, 40 for course, and 40 for evaluation).

Professor Jette Sandholm Kastrup, Department of Medicinal Chemistry at the Faculty of Pharmaceutical Sciences, University of Copenhagen.

Total course fee: DKK 10,700 (including lunch),

of which operating costs: DKK 1,500.

1 March 2012.

16 participants.

Conditions for participation: The course is primarily offered to PhD students who have completed undergraduate courses in biochemistry, biology, chemistry, molecular biology, pharmacology, or pharmacy, or researchers within the pharmaceutical industry.

Applicants enrolled in part-time master's programs at the Faculty of Pharmaceutical Sciences, University of Copenhagen may participate in the course.