3kt5

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Crystal Structure of N88S mutant HIV-1 ProteaseCrystal Structure of N88S mutant HIV-1 Protease

Structural highlights

3kt5 is a 1 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:3kt2
Gene:gag-pol (Human immunodeficiency virus 1)
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Nelfinavir is an inhibitor of HIV-1 protease, and is used for treatment of patients suffering from HIV/AIDS. However, treatment results in drug resistant mutations in HIV-1 protease. N88D and N88S are two such mutations which occur in the non-active site region of the enzyme. We have determined crystal structures of unliganded N88D and N88S mutants of HIV-1 protease to resolution of 1.65A and 1.8A, respectively. These structures refined against synchrotron data lead to R-factors of 0.1859 and 0.1780, respectively. While structural effects of N88D are very subtle, the mutation N88S has caused a significant conformational change in D30, an active site residue crucial for substrate and inhibitor binding.

Resistance mechanism revealed by crystal structures of unliganded nelfinavir-resistant HIV-1 protease non-active site mutants N88D and N88S.,Bihani SC, Das A, Prashar V, Ferrer JL, Hosur MV Biochem Biophys Res Commun. 2009 Nov 13;389(2):295-300. Epub 2009 Aug 29. PMID:19720046[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Bihani SC, Das A, Prashar V, Ferrer JL, Hosur MV. Resistance mechanism revealed by crystal structures of unliganded nelfinavir-resistant HIV-1 protease non-active site mutants N88D and N88S. Biochem Biophys Res Commun. 2009 Nov 13;389(2):295-300. Epub 2009 Aug 29. PMID:19720046 doi:10.1016/j.bbrc.2009.08.138

3kt5, resolution 1.80Å

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