Download MendeleyEnzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design.
Engh, R.A., Brandstetter, H., Sucher, G., Eichinger, A., Baumann, U., Bode, W., Huber, R., Poll, T., Rudolph, R., von der Saal, W.(1996) Structure 4: 1353-1362
- PubMed: 8939759
- DOI: https://doi.org/10.1016/s0969-2126(96)00142-6
- Primary Citation of Related Structures:
1UVS, 1UVT, 1UVU - PubMed Abstract:
The explosive growth in the rate of X-ray determination of protein structures is fuelled largely by the expectation that structural information will be useful for pharmacological and biotechnological applications. For example, there have been intensive efforts to develop orally administrable antithrombotic drugs using information about the crystal structures of blood coagulation factors, including thrombin. Most of the low molecular weight thrombin inhibitors studied so far are based on arginine and benzamidine. We sought to expand the database of information on thrombin-inhibitor binding by studying new classes of inhibitors.
Organizational Affiliation:
Max-Planck-Institut für Biochemie, D82152 Martinsried, Germany. engh@biochem.mpg.de
