2jo0
From Proteopedia
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'''The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1'''<br /> | '''The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JO0 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]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http:// | + | 2JO0 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]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JO0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: virus/viral protein complex]] | [[Category: virus/viral protein complex]] | ||
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Revision as of 12:20, 23 January 2008
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The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1
Overview
The protein CA forms the mature capsid of human immunodeficiency virus., Hexamerization of the N-terminal domain and dimerization of the C-terminal, domain, CAC, occur during capsid assembly, and both domains constitute, potential targets for anti-HIV inhibitors. CAC homodimerization occurs, mainly through its second helix, and is abolished when its sole tryptophan, is mutated to alanine. Previous thermodynamic data obtained with the, dimeric and monomeric forms of CAC indicate that the structure of the, mutant resembles that of a monomeric intermediate found in the folding and, association reactions of CAC. We have solved the three-dimensional, structure in aqueous solution of the monomeric mutant. The structure is, similar to that of the subunits in the dimeric, nonmutated CAC, except the, segment corresponding to the second helix, which is highly dynamic. At the, end of this region, the polypeptide chain is bent to bury several, hydrophobic residues and, as a consequence, the last two helices are, rotated 90 degrees when compared to their position in dimeric CAC. The, previously obtained thermodynamic data are consistent with the determined, structure of the monomeric mutant. This extraordinary ability of CAC to, change its structure may contribute to the different modes of association, of CA during HIV assembly, and should be taken into account in the design, of new drugs against this virus.
About this Structure
2JO0 is a Single protein structure of sequence from Human immunodeficiency virus 1. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.
Reference
Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein., Alcaraz LA, Del Alamo M, Barrera FN, Mateu MG, Neira JL, Biophys J. 2007 Aug 15;93(4):1264-76. Epub 2007 May 25. PMID:17526561
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