1hvc

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[[Image:1hvc.gif|left|200px]]
[[Image:1hvc.gif|left|200px]]
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{{Structure
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|PDB= 1hvc |SIZE=350|CAPTION= <scene name='initialview01'>1hvc</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1hvc", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=A79:N-{1-BENZYL-(2S,3S)-2,3-DIHYDROXY-4-[3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRYLAMINO]-5-PHENYL-PENTYL}-3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRAMIDE'>A79</scene>
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|GENE= SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])
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{{STRUCTURE_1hvc| PDB=1hvc | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvc OCA], [http://www.ebi.ac.uk/pdbsum/1hvc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hvc RCSB]</span>
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'''CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR'''
'''CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR'''
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[[Category: Bhat, T N.]]
[[Category: Bhat, T N.]]
[[Category: Erickson, J W.]]
[[Category: Erickson, J W.]]
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[[Category: hydrolase(acid protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:16:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:56 2008''
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Revision as of 16:16, 2 May 2008

Template:STRUCTURE 1hvc

CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR


Overview

HIV-1 proteinase (HIV PR) is a dimeric enzyme composed of two identical polypeptide chains that associate with twofold symmetry. We have determined to 1.8 A the crystal structure of a covalently tethered dimer of HIV PR. The tethered dimer:inhibitor complex is identical in nearly every respect to the complex of the same inhibitor with the wild type dimeric molecule, except for the linker region. Our results suggest that the tethered dimer may be a useful surrogate enzyme for studying the effects of single site mutations on substrate and inhibitor binding as well as on enzyme asymmetry, and for simulating independent mutational drift of the two domains which has been proposed to have led to the evolution of modern day, single-chain aspartic proteinases.

About this Structure

1HVC is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor., Bhat TN, Baldwin ET, Liu B, Cheng YS, Erickson JW, Nat Struct Biol. 1994 Aug;1(8):552-6. PMID:7664084 Page seeded by OCA on Fri May 2 19:16:17 2008

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