Analysis of the contact interfaces of HIV reverse transcriptase subunits

Autor:	Veselovskiĭ Av, Belov Da
Rok vydání:	2007
Předmět:	Stereochemistry Dimer Protein subunit Clinical Biochemistry Binding energy Human immunodeficiency virus (HIV) Protein dimer medicine.disease_cause Biochemistry Reverse transcriptase chemistry.chemical_compound chemistry medicine Molecular Medicine Bioorganic chemistry Contact area
Zdroj:	Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry. 1:9-16
ISSN:	1990-7516 1990-7508
DOI:	10.1134/s1990750807010027
Popis:	Analysis of structure and features of subunit contact areas of HIV reverse transcriptase (RT) was done. The amino acid residues from contact areas of RT subunits are more conservative than the other residues of this protein. Estimation of contribution of the amino acid residues from the contact areas into the binding energy of subunits showed that the binding energy is mostly localized on the several amino acid residues of the dimer interface (hot spots). The majority of these hot spots form several clusters on the contact surfaces. Analysis of these clusters allows prediction of the region on the contact area of the protein dimer that can be useful for design RT HIV inhibitors of dimerization.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1044f4906c9535986305ccb07e2d3297 https://doi.org/10.1134/s1990750807010027 Zobrazit plný text záznamu Full text from SpringerLink