1hvc: Difference between revisions

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[[Image:1hvc.~~gif~~|left|200px]]

[[Image:1hvc.png|left|200px]]

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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===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_7664084}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7664084 is the PubMed ID number.

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==About this Structure==

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[[Category: Bhat, T N.]]

[[Category: Erickson, J W.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:16:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:50:38 2008''

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-[[Image:1hvc.gif|left|200px]]
+{{Seed}}
+[[Image:1hvc.png|left|200px]]
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 {{STRUCTURE_1hvc|  PDB=1hvc  |  SCENE=  }}
-'''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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664084}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664084 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7664084}}
 ==About this Structure==
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 [[Category: Bhat, T N.]]
 [[Category: Erickson, J W.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:16:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:50:38 2008''