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TitleComputational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease
Journal, issue, pagesProteins, Vol. 70, Page 678-694, Year 2007
Publish dateNov 17, 2006 (structure data deposition date)
AuthorsAltman, M.D. / Nalivaika, E.A. / Prabu-Jeyabalan, M. / Schiffer, C.A. / Tidor, B.
External linksProteins / PubMed:17729291
MethodsX-ray diffraction
Resolution2 - 2.25 Å
Structure data

PDB-2nxd:
Structure of HIV-1 protease D25N complexed with rt-rh analogue peptide GLY-ALA-ASP-ILE-PHE*TYR-LEU-ASP-GLY-ALA
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2nxl:
Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide GLY-ALA-GLU-VAL-PHE*TYR-VAL-ASP-GLY-ALA
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2nxm:
Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide GLY-ALA-GLN-THR-PHE*TYR-VAL-ASP-GLY-ALA
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • hiv-1 m:b_arv2/sf2 (virus)
KeywordsHYDROLASE/HYDROLASE SUBSTRATE / peptide design; molecular dynamics; hiv protease; substrate recognition; calorimetry / HYDROLASE-HYDROLASE SUBSTRATE COMPLEX

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