1hvc

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(New page: 200px<br /> <applet load="1hvc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hvc, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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caption="1hvc, resolution 1.8&Aring;" />
caption="1hvc, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR'''<br />
'''CRYSTAL STRUCTURE OF A TETHERED DIMER OF HIV-1 PROTEASE COMPLEXED WITH AN INHIBITOR'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1HVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with A79 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HVC OCA].
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1HVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=A79:'>A79</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVC OCA].
==Reference==
==Reference==
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[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baldwin, E.T.]]
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[[Category: Baldwin, E T.]]
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[[Category: Bhat, T.N.]]
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[[Category: Bhat, T N.]]
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[[Category: Erickson, J.W.]]
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[[Category: Erickson, J W.]]
[[Category: A79]]
[[Category: A79]]
[[Category: hydrolase(acid protease)]]
[[Category: hydrolase(acid protease)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:07:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:16 2008''

Revision as of 11:05, 21 February 2008


1hvc, resolution 1.8Å

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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 with as ligand. 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

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