caa a22 4500 378920081 CHVBK 20180305123603.0 cr unu---uuuuu 161128e20040413xx s 000 0 eng 10.1515/BC.2004.026 doi (NATIONALLICENCE)gruyter-10.1515/BC.2004.026 The central domain of the matrix protein of HIV-1: influence on protein structure and virus infectivity [Elektronische Daten] [A.-D. Ellenrieder, W. Kremer, B. Kattenbeck, O. Hantschel, G. Horn, H. R. Kalbitzer, S. Modrow] The central region of the matrix protein p17 of HIV-1 is known to be essential during virus assembly. We substituted alanines for amino acid triplets in this region of p17 (amino acid residues 47 to 55: NPG LLE TSE). Introduction of the respective mutations into the gag-coding sequence of HIproviruses and subsequent transfection into Cos-7 cells led to particle production and release. Exchange of LLE resulted in the production of noninfectious particles. These residues may be important for correct folding and assembly of the processed matrix protein and the production of infectious HIV. In vitro studies of wildtype and mutated matrix proteins using spectroscopic methods (NMR, fluorescence, CD) yielded detailed data about structure and stability. Two-dimensional NMR spectroscopy showed that wildtype and mutant proteins (p17-NPG and p17-TSE) are well folded. Besides structural changes at the mutated site, chemical shift changes indicate small but significant long range structural rearrangements. The stability against chemically and thermally induced unfolding of the mutants p17-NPG and p17-TSE was slightly decreased, while that of p17-LLE was drastically diminished. The alterations have only a local effect on protein folding for the mutants p17-NPG and p17-TSE, and the globular tertiary structure remains nearly unchanged. For p17-LLE, however, the substitutions seem to trigger significant changes in structural elements. Copyright © 2004 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Ellenrieder A.-D aut Kremer W. aut Kattenbeck B. aut Hantschel O. aut Horn G. aut Kalbitzer H. R. aut Modrow S. aut Biological Chemistry Walter de Gruyter 385/3-4(2004-04-13), 303-313 1431-6730 385:3-4<303 2004 385 bchm https://doi.org/10.1515/BC.2004.026 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2004.026 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ellenrieder A.-D aut NATIONALLICENCE 700 1- Kremer W. aut NATIONALLICENCE 700 1- Kattenbeck B. aut NATIONALLICENCE 700 1- Hantschel O. aut NATIONALLICENCE 700 1- Horn G. aut NATIONALLICENCE 700 1- Kalbitzer H. R. aut NATIONALLICENCE 700 1- Modrow S. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 385/3-4(2004-04-13), 303-313 1431-6730 385:3-4<303 2004 385 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter