2je4

From Proteopedia

Revision as of 15:26, 30 October 2007

ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF CHEMICALLY-SYNTHESIZED HIV-1 PROTEASE IN COMPLEX WITH JG-365

Overview

As part of our ongoing studies of the human immunodeficiency virus type 1, (HIV-1) protease enzyme, we set out to develop a modular chemical, synthesis of the protein from multiple peptide segments. Our initial, attempts were frustrated by the insolubility of intermediate peptide, products. To overcome this problem, we designed a synthetic strategy, combining the solubility-enhancing properties of C-terminal (Arg)n tags, and the biological phenomenon of autoprocessing of the Gag-Pol polyprotein, that occurs during maturation of the HIV-1 virus in vivo. Synthesis of a, 119-residue peptide chain containing 10 residues of the reverse, transcriptase (RT) open reading frame plus an (Arg)10 tag at the, C-terminus was straightforward by native chemical ligation followed by, conversion of the Cys ... [(full description)]

About this Structure

2JE4 is a [Protein complex] structure of sequences from [Human immunodeficiency virus 1] with ACT, SO4 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Modular Total Chemical Synthesis of a Human Immunodeficiency Virus Type 1 Protease., Johnson EC, Malito E, Shen Y, Rich D, Tang WJ, Kent SB, J Am Chem Soc. 2007 Sep 19;129(37):11480-11490. Epub 2007 Aug 18. PMID:17705484

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