1u8g

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Revision as of 12:26, 8 November 2007

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spinqualitylabelsall models 1u8g, resolution 2.201Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of a HIV-1 Protease in complex with peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2

Overview

Depending on the excess of ligand used for complex formation, the HIV-1, protease complexed with a novel phenylnorstatine inhibitor forms crystals, of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The, orthorhombic form shows an unusual complexity of crystal packing: in, addition to one inhibitor molecule that is bound to the enzyme active, site, the second inhibitor molecule is bound as an outer ligand at the, protein interface. Binding of the outer ligand apparently increases the, crystal-quality parameters so that the diffraction data allow solution of, the structure of the complex at 1.03 A, the best resolution reported to, date. The outer ligand interacts with all four surrounding HIV-1 protease, molecules and has a bent conformation owing to its accommodation in the, intermolecular space. The parameters of the solved structures of the, orthorhombic and hexagonal forms are compared.

About this Structure

1U8G is a Single protein structure of sequence from Human immunodeficiency virus 1 with NH2 as ligand. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.

Reference

Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex., Brynda J, Rezacova P, Fabry M, Horejsi M, Stouracova R, Soucek M, Hradilek M, Konvalinka J, Sedlacek J, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1943-8. Epub 2004, Oct 20. PMID:15502300

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