Peptide Mimetic Factor VIIa Inhibitor: Importance of Hydrophilic Pocket in S2 Site to Improve Selectivity Against Thrombin

Title: Peptide Mimetic Factor VIIa Inhibitor: Importance of Hydrophilic Pocket in S2 Site to Improve Selectivity Against Thrombin

Volume: 2 Issue: 3

Author(s): S. Kadono, A. Sakamoto, Y. Kikuchi, M. Oh-eda, N. Yabuta, T. Koga, K. Hattori, T. Shiraishi, M. Haramura and H. Kodama

Affiliation:

Keywords: factor vIIa, blood coagulation, antithrombotic, serine protease, x-ray crystallography, drug design

Abstract: X-ray structure analysis of human factor VIIa/soluble tissue factor in complex with a peptide mimetic inhibitor reveals that Asp60, Tyr94, and Thr98 in the S2 site play an important role for the improvement of selectivity against thrombin.

Cite this article as:

Kadono S., Sakamoto A., Kikuchi Y., Oh-eda M., Yabuta N., Koga T., Hattori K., Shiraishi T., Haramura M. and Kodama H., Peptide Mimetic Factor VIIa Inhibitor: Importance of Hydrophilic Pocket in S2 Site to Improve Selectivity Against Thrombin, Letters in Drug Design & Discovery 2005; 2 (3) . https://dx.doi.org/10.2174/1570180053765200