ÿþ<!doctype html public "-//w3c//dtd html 3.2//en"> <html> <head> <title>APJMBB Volume 15 Number 2, June 2007</title> <meta name="GENERATOR" content="Arachnophilia 4.0"> <meta name="FORMATTER" content="Arachnophilia 4.0"> </head> <STYLE TYPE="text/css"> .head { font-family: Arial narrow, Times new roman, Verdana, Helvetica, sans-serif; font-size: 11pt; color: #000000; font-style: italic;} .title { font-family: Times new roman, Verdana, Arial, Helvetica, sans-serif; font-size: 14pt; color: #000000; font-weight: bold;} .text { font-family: Times new roman, Verdana, Arial, Helvetica, sans-serif; font-size: 12pt; color: #000000;} .affil { font-family: Times new roman, Verdana, Arial, Helvetica, sans-serif; font-size: 11pt; color: #000000; font-style: italic;} .sechead { font-family: Times new roman, Verdana, Arial, Helvetica, sans-serif; font-size: 12pt; color: #000000; font-weight: bold;} A {text-decoration:none} A:hover {color:#ff8040;} .text3 { font-family: Verdana, Arial, Helvetica, sans-serif; font-size: 9pt; color: #000000;} .text4 { font-family: Verdana, Arial, Helvetica, sans-serif; font-size: 9pt; color: #0000ff;} .text2 { font-family: Times new roman, Verdana, Arial, Helvetica, sans-serif; font-size: 9pt; color: #000000;} </STYLE> <body bgcolor="#ffffff" text="#000000" link="#0000ff" vlink="#800080" alink="#ff0000"> <img src="../images/apjlogos.gif" width="125" height="87" alt=""><br><hr width=90% align=left> <span class=text3><a href="152cont.htm">[ Contents ]</a> <a href="152a.htm">[ Previous abstract ]</a> <a href="152c.htm">[ Next abstract ]</a> <a href="../html151/151cont.htm">[ Previous issue ]</a> [ Next issue ] [ <a href="../../apjhome.htm">APJMBB home</a> ]</span><hr width=90% align=left> <p class=head>As. Pac. J. Mol. Biol. &amp; Biotech., June 2007 Vol. 15, x-x</p> <table width="90%" border="0" cellspacing="0" cellpadding="5"> <tr> <td width=100% valign=top><span class=title>Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors </span><br> <br> <span class=text>Lee Yean Kee<sup>1</sup>, Tan Siew Kiat<sup>2</sup>, Habibah Abdul Wahab<sup>3</sup>, Rohana Yusof<sup>4</sup> and Noorsaadah Abd. Rahman<sup>1</sup>* </span><br> <br> <span class=affil><sup>1</sup>Department of Chemistry, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur<br> <sup>2</sup>Institute of Biological Sciences, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur<br> <sup>3</sup>School of Pharmacy, Universiti Sains Malaysia, Pulau Pinang<br> <sup>4</sup>Dept. of Mol. Medicine, Faculty of Medicine, Universiti Malaya, 50603 Kuala Lumpur </span> <p class=text2>*Author for Correspondence.<br> Dept. of Chemistry, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur. Malaysia<br>Tel: (603)79674254, Fax: (603)79674193, Email: noorsaadah@um.edu.my </p> <p class=text align=justify><span class=sechead>Abstract.</span><br> The protein-ligand binding interactions studies were carried out by performing dockings of the ligands that were found to be competitively inhibiting the activities of the DEN2 NS2B/NS3 serine protease onto the catalytic triad of a model of DEN2 NS2B/NS3 protease. Results indicate the importance of three out of the five residues reported to be essential for binding activities of the NS2B/NS3 serine protease. These residues are Tyr-150, Asn-152 and Gly-153. In addition, Ser-135 and Gly-151 were also found to be very important in forming hydrogen bonds with the inhibitors. Moreover, Ser-131, Pro-132, Tyr-150 and Asn-152 were found to be important for van der Waals interaction of the ligand, while Val-52, Leu-128, Pro-132 and Val-155 are involved in hydrophobic interaction with the inhibitors. </p> <a href="152b.pdf" class=text4>[Get pdf]</a> </td></tr></table> <br> <br> <br> <br> </body> </html>