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Literature DB >> 1946342

Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases.

Abstract

The different isolates available for HIV-1 and HIV-2 were compared for the region of the protease (PR) sequence, and the variations in amino acids were analyzed with respect to the crystal structure of HIV-1 PR with inhibitor. Based on the extensive homology (39 identical out of 99 residues), models were built of the HIV-2 PR complexed with two different aspartic protease inhibitors, acetylpepstatin and a renin inhibitor, H-261. Comparison of the HIV-1 PR crystal structure and the HIV-2 PR model structure and the analysis of the changes found in different isolates showed that correlated substitutions occur in the hydrophobic interior of the molecule and at surface residues involved in ionic or hydrogen bond interactions. The substrate binding residues of HIV-1 and HIV-2 PRs show conservative substitutions of four residues. The difference in affinity of HIV-1 and HIV-2 PRs for the two inhibitors appears to be due in part to the change of Val 32 in HIV-1 PR to Ile in HIV-2 PR.

Entities: Chemical Disease Species

Mesh：

Substances：
HIV Protease

Year: 1991 PMID： 1946342 DOI： 10.1002/prot.340100406

Source DB: PubMed Journal: Proteins ISSN： 0887-3585

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Cited

30 in total

1. Emergence of drug resistance mutations in human immunodeficiency virus type 2-infected subjects undergoing antiretroviral therapy.

Authors: B Rodés; A Holguín; V Soriano; M Dourana; K Mansinho; F Antunes; J González-Lahoz
Journal: J Clin Microbiol Date: 2000-04 Impact factor: 5.948

2. Structure of RC1339/APRc from Rickettsia conorii, a retropepsin-like aspartic protease.

Authors: Mi Li; Alla Gustchina; Rui Cruz; Marisa Simões; Pedro Curto; Juan Martinez; Carlos Faro; Isaura Simões; Alexander Wlodawer
Journal: Acta Crystallogr D Biol Crystallogr Date: 2015-09-30

3. Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors.

Authors: Michel Ntemgwa; Bluma G Brenner; Maureen Oliveira; Daniela Moisi; Mark A Wainberg
Journal: Antimicrob Agents Chemother Date: 2006-11-20 Impact factor: 5.191

10. In vitro isolation and identification of human immunodeficiency virus (HIV) variants with reduced sensitivity to C-2 symmetrical inhibitors of HIV type 1 protease.

Authors: M J Otto; S Garber; D L Winslow; C D Reid; P Aldrich; P K Jadhav; C E Patterson; C N Hodge; Y S Cheng
Journal: Proc Natl Acad Sci U S A Date: 1993-08-15 Impact factor: 11.205

Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases.

1. Emergence of drug resistance mutations in human immunodeficiency virus type 2-infected subjects undergoing antiretroviral therapy.

2. Structure of RC1339/APRc from Rickettsia conorii, a retropepsin-like aspartic protease.

3. Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors.

4. Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease.

5. Cross-linked peptoid-based dimerization inhibitors of HIV-1 protease.

6. Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors.

7. Hematopoietic cytokines: similarities and differences in the structures, with implications for receptor binding.

8. Synthetic "interface" peptides alter dimeric assembly of the HIV 1 and 2 proteases.

9. Structure of equine infectious anemia virus proteinase complexed with an inhibitor.

10. In vitro isolation and identification of human immunodeficiency virus (HIV) variants with reduced sensitivity to C-2 symmetrical inhibitors of HIV type 1 protease.