2jo0: Difference between revisions

Revision as of 16:54, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jo0.png

Template:STRUCTURE 2jo0

The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1

Template:ABSTRACT PUBMED 17526561

About this StructureAbout this Structure

2JO0 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17526561}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17526561 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17526561}}
 ==About this Structure==
-JO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JO0 OCA].
+JO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JO0 OCA].
 ==Reference==
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 [[Category: Monomer]]
 [[Category: Virus/viral protein complex]]
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