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Analysis of the structure of chemically synthesized HIV-1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 Å data

✍ Scribed by Maria Miller; Maciej Geller; Michael Gribskov; Stephen B. H. Kent

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 294 KB
Volume: 27
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199702)27:2<184::aid-prot4>3.0.co;2-g

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✦ Synopsis

The structure of a complex between a hexapeptide-based inhibitor, MVT-101, and the chemically synthesized (Aba 67,95,167,195; Aba: L-a-amino-n-butyric acid) protease from the human immunodeficiency virus (HIV-1), reported previously at 2.3 Å has now been refined to a crystallographic R factor of 15.4% at 2.0 Å resolution. Root mean square deviations from ideality are 0.18 Å for bond lengths and 2.4°for the angles. The inhibitor can be fitted to the difference electron density map in two alternative orientations. Drastic differences are observed for positions and interactions at P3/S3 and P38/S38 subsites of the two orientations due to different crystallographic environments. Proteins 27:184-194

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Analysis of the structure of HIV-1 protease complexed with a hexapeptide inhibitor. Part II: Molecular dynamic studies of the active site region

✍ Maciej Geller; Maria Miller; Stanley M. Swanson; Jacob Maizel 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 130 KB 👁 2 views

Six models of the catalytic site of HIV-1 protease complexed with a reduced peptide inhibitor, MVT-101, were investigated. These studies focused on the details of protonation of the active site, its total net charge and hydrogen bonding pattern, which was consistent with both the observed coplanar c