2b7f
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(New page: 200px<br /><applet load="2b7f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b7f, resolution 2.60Å" /> '''Crystal structure of...)
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Revision as of 06:29, 21 November 2007
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Crystal structure of human T-cell leukemia virus protease, a novel target for anti-cancer design
Overview
The successful development of a number of HIV-1 protease (PR) inhibitors, for the treatment of AIDS has validated the utilization of retroviral PRs, as drug targets and necessitated their detailed structural study. Here we, report the structure of a complex of human T cell leukemia virus type 1, (HTLV-1) PR with a substrate-based inhibitor bound in subsites P5 through, P5'. Although HTLV-1 PR exhibits an overall fold similar to other, retroviral PRs, significant structural differences are present in several, loop areas, which include the functionally important flaps, previously, considered to be structurally highly conserved. Potential key residues, responsible for the resistance of HTLV-1 PR to anti-HIV drugs are, identified. We expect that the knowledge accumulated during the, development of anti-HIV drugs, particularly in overcoming drug resistance, will help in designing a novel class of antileukemia drugs targeting, HTLV-1 PR and in predicting their drug-resistance profile. The structure, presented here can be used as a starting point for the development of such, anticancer therapies.
About this Structure
2B7F is a Single protein structure of sequence from Human t-cell leukemia virus type i with PO4 and ACE as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design., Li M, Laco GS, Jaskolski M, Rozycki J, Alexandratos J, Wlodawer A, Gustchina A, Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18332-7. Epub 2005 Dec 13. PMID:16352712
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