Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Crystal structure of an FIV/HIV chimeric protease complexed with the broad-based inhibitor, TL-3. | Retrovirology BioMed Central Research Crystal structure of an FIV HIV chimeric protease complexed with the broad-based inhibitor TL-3 Holly Heaslet1 Ying-Chuan Lin2 Karen Tam2 Bruce E Torbett3 John H Elder2 and C David Stout 2 Open Access Address 1Pfizer Global Research Development 2800 Plymouth Rd. Ann Arbor MI 48105 USA 2Department of Molecular Biology The Scripps Research Institute 10550 N. Torrey Pines Rd. La Jolla CA 92037 USA and 3Department of Molecular Experimental Medicine The Scripps Research Institute 10550 N. Torrey Pines Rd. La Jolla CA 92037 USA Email Holly Heaslet - hheaslet@ Ying-Chuan Lin - ylin@ Karen Tam - ktam@ Bruce E Torbett - betorbet@ John H Elder - jelder@ C David Stout - dave@ Corresponding author Published 09 January 2007 Received 14 September 2006 Accepted 09 January 2007 Retrovirology 2007 4 1 doi l742-4690-4-l p This article is available from http content 4 l l 2007 Heaslet et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract We have obtained the Ả crystal structure of FIV protease PR in which l2 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR l2X FIV PR . The chimeric PR was crystallized in complex with the broad-based inhibitor TL-3 which inhibits wild type FIV and HIV PRs as well as l2X FIV PR and several drug-resistant HIV mutants l-4 . Biochemical analyses have demonstrated that TL-3 inhibits these PRs in the order HIV PR l2X FIV PR FIV pR with Kị values of nM l0 nM and 4l nM respectively 2-4 . Comparison of the crystal structures .
