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  Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain

Divita, G., Restle, T., Goody, R. S., Chermann, J. C., & Baillon, J. G. (1994). Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. The Journal of Biological Chemistry, 269(18), 13080-13083. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7513698.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A912-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C219-7
Genre: Journal Article

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JBiolChem_269_1994_13080.pdf (Any fulltext), 522KB
 
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Divita, Gilles1, Author              
Restle, Tobias1, 2, Author              
Goody, Roger S.1, Author              
Chermann, J. C., Author
Baillon, J. G., Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Based on presently available information on the structure of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, peptides have been synthesized which correspond to the sequence of a particular region of the protein involved in formation of the active heterodimeric form of the enzyme. Several peptides that are 15-19 amino acids long and that are derived from the so-called connection domain of the reverse transcriptase are able to inhibit dimerization of the enzyme and thus inhibit development of its enzymatic activities. In particular, a tryptophan-rich 19-mer corresponding to residues 389-407 was relatively efficient, showing an apparent dissociation constant in the micromolar range for one or both of the subunits. The sequence of this region is identical for both subunits, since one (molecular mass of 51 kDa) is the proteolytic product of the other (molecular mass of 66 kDa). Dissociation of the preformed heterodimer could not be induced by the peptides, but increasing concentrations reduced the rate of dimerization in a concentration-dependent manner until it became immeasurable at high concentrations. The results suggest that inhibition of dimerization of reverse transcriptase is an attractive approach to chemotherapeutic intervention in HIV infection and that further development of peptide-based inhibition strategies is worth pursuing.

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Language(s): eng - English
 Dates: 1994-03-101994-05-06
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 269 (18) Sequence Number: - Start / End Page: 13080 - 13083 Identifier: ISSN: 0021-9258
CoNE: /journals/resource/954925410826_1