1fqx
From Proteopedia
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(New page: 200px<br /> <applet load="1fqx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqx, resolution 3.1Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:57, 8 November 2007
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CRYSTAL STRUCTURE OF THE COMPLEX OF HIV-1 PROTEASE WITH A PEPTIDOMIMETIC INHIBITOR
Overview
Crystallization conditions for an HIV-1 protease-inhibitor complex were, optimized to produce crystals suitable for X-ray diffraction experiments., The X-ray structure of the HIV-1 protease complex was solved and refined, at 3.1 A resolution. In contrast to Saquinavir, the mimetic hydroxy group, of the inhibitor Boc-Phe-Psi[(S)-CH(OH)CH(2)NH]-Phe-Glu-Phe-NH(2) is, placed asymmetrically with respect to the non-crystallographic twofold, axis of the protease dimer so that hydrogen bonds between the amino group, of the inhibitor and the catalytic aspartates can be formed. The inhibitor, binds in the centre of the active site by a compact network of hydrogen, bonds to Gly27, Gly127, Asp25, Asp125 and via the buried water molecule, W301 to Ile50 and Ile150.
About this Structure
1FQX is a Single protein structure of sequence from Human immunodeficiency virus with NH2 as ligand. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.
Reference
A distinct binding mode of a hydroxyethylamine isostere inhibitor of HIV-1 protease., Dohnalek J, Hasek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Brynda J, Sedlacek J, Fabry M, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):472-6. PMID:11223536
Page seeded by OCA on Thu Nov 8 14:03:43 2007
Categories: HIV-1 retropepsin | Human immunodeficiency virus | Single protein | Brynda, J. | Dohnalek, J. | Duskova, J. | Fabry, M. | Hasek, J. | Hradilek, M. | Konvalinka, J. | Petrokova, H. | Sedlacek, J. | Soucek, M. | NH2 | Aspartyl protease | Drug design | Hiv | Hydroxyethylamine isostere | Inhibitor | Peptidomimetic | Protease
