The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU
| Autor: | Silvia Spinelli, Pedro M. Alzari, Roberto J. Poljak, Q Z Liu, P H Hirel |
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| Přispěvatelé: | Immunobiologie, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Département Biotechnologie, Rhóne-Poulenc Rorer, This research was funded by grants from the Institut Pasteur, CNRS, ANRS and Rhone-Poulenc Rorer., Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 1991 |
| Předmět: |
Models
Molecular Protein Conformation [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] medicine.medical_treatment [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology medicine.disease_cause 01 natural sciences Biochemistry Inclusion bodies MESH: HIV-1 MESH: HIV Protease 03 medical and health sciences MESH: Protein Conformation Protein structure HIV Protease X-Ray Diffraction MESH: Computer Simulation protein folding 0103 physical sciences Escherichia coli [CHIM.CRIS]Chemical Sciences/Cristallography medicine Computer Simulation MESH: Cloning Molecular [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Denaturation (biochemistry) Cloning Molecular X-ray crystallography 030304 developmental biology chemistry.chemical_classification HIV-1 aspartyl protease BRU 0303 health sciences Protease [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] 010304 chemical physics MESH: Escherichia coli MESH: X-Ray Diffraction General Medicine 3. Good health Amino acid Enzyme chemistry HIV-1 Protein folding [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM] MESH: Models Molecular |
| Zdroj: | Biochimie Biochimie, 1991, 73 (11), pp.1391-1396. ⟨10.1016/0300-9084(91)90169-2⟩ Biochimie, Elsevier, 1991, 73 (11), pp.1391-1396. ⟨10.1016/0300-9084(91)90169-2⟩ |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/0300-9084(91)90169-2 |
| Popis: | International audience; The crystal structure of the aspartyl protease encoded by the gene pol of the human immunodeficiency virus (HIV-1, isolate BRU) has been determined to 2.7 A resolution. The enzyme, expressed as an insoluble denatured polypeptide in inclusion bodies of Escherichia coli has been renatured and crystallized. It differs by several amino acid replacements from the homologous enzymes of other HIV-1 isolates. A superposition of the C alpha-backbone of the BRU protease with that of the SF2 protease gives a roots mean square positional difference of 0.45 A. Thus, neither the denaturation/renaturation process nor the amino acid replacements have a noticeable effect on the three-dimensional structure of the BRU protease or on the detailed conformation of the catalytic site, which is very similar to that of other aspartyl proteases. |
| Databáze: | OpenAIRE |
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