3k4v | pdb_00003k4v

New crystal form of HIV-1 Protease/Saquinavir structure reveals carbamylation of N-terminal proline

spinqualitylabelsall models 3k4v, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3k4v is a 4 chain structure with sequence from Hiv-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, DMS, ROC NonStd Res: ARF Gene: gag-pol (HIV-1) Activity: HIV-1 retropepsin, with EC number 3.4.23.16 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 Protein carbamylation is of great concern both in vivo and in vitro. Here, we report the first structural characterization of a protein carbamylated at the N-terminal proline. The unexpected carbamylation of the alpha-amino group of the least reactive codified amino acid has been detected in high-resolution electron density maps of a new crystal form of the HIV-1 protease/saquinavir complex. The carbamyl group is found coplanar to the proline ring with a trans conformation. The reaction of N-terminal with cyanate ion derived from the chaotropic agent urea was confirmed by mass spectra analysis on protease single crystals. Implications of carbamylation process in vitro and in vivo are discussed. Carbamylation of N-terminal proline.,Olajuyigbe FM, Demitri N, Ajele JO, Maurizio E, Randaccio L, Geremia S ACS Med Chem Lett. 2010 Jun 2;1(6):254-7. doi: 10.1021/ml100046d. eCollection, 2010 Sep 9. PMID:24900204 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus protease

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