1wkn: Difference between revisions

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~~{{Theoretical_model}}~~

==A PLAUSIBLE MODEL OF FULL-LENGTH INTEGRASEDNA COMPLEX==

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WKN FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wkn FirstGlance], [http://www.ebi.ac.uk/pdbsum/1wkn PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

A model of the full-length HIV-1 integrase dimer was constructed assembling the experimentally determined structures of the single domains. Subsequently, the three-domain protein-viral DNA complex was generated for the first time through an automated docking algorithm, obtained modifying the ESCHER program, a well-known method for protein-protein docking. A detailed study of the contacts established with DNA by the enzyme revealed that the predicted model reproduced the results of mutagenesis and cross-linking experiments, confirming the validity of our docking approach in predicting the base specificity in the DNA-protein interaction.

~~[[Image~~:~~1wkn~~.~~png|left|200px]]~~

Analysis of the full-length integrase-DNA complex by a modified approach for DNA docking.,De Luca L, Pedretti A, Vistoli G, Barreca ML, Villa L, Monforte P, Chimirri A Biochem Biophys Res Commun. 2003 Oct 31;310(4):1083-8. PMID:14559226<ref>PMID:14559226</ref>

~~{{STRUCTURE_1wkn| PDB=1wkn | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~===A PLAUSIBLE MODEL OF FULL-LENGTH INTEGRASEDNA COMPLEX===~~

== References ==

~~{{ABSTRACT_PUBMED_14559226}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:014559226<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Barreca, M L]]

[[Category: Chimirri, A]]

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@@ Line 1: / Line 1: @@
-{{Theoretical_model}}
+==A PLAUSIBLE MODEL OF FULL-LENGTH INTEGRASEDNA COMPLEX==
+<StructureSection load='1wkn' size='340' side='right' caption='[[1wkn]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WKN FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wkn FirstGlance], [http://www.ebi.ac.uk/pdbsum/1wkn PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A model of the full-length HIV-1 integrase dimer was constructed assembling the experimentally determined structures of the single domains. Subsequently, the three-domain protein-viral DNA complex was generated for the first time through an automated docking algorithm, obtained modifying the ESCHER program, a well-known method for protein-protein docking. A detailed study of the contacts established with DNA by the enzyme revealed that the predicted model reproduced the results of mutagenesis and cross-linking experiments, confirming the validity of our docking approach in predicting the base specificity in the DNA-protein interaction.
-[[Image:1wkn.png|left|200px]]
+Analysis of the full-length integrase-DNA complex by a modified approach for DNA docking.,De Luca L, Pedretti A, Vistoli G, Barreca ML, Villa L, Monforte P, Chimirri A Biochem Biophys Res Commun. 2003 Oct 31;310(4):1083-8. PMID:14559226<ref>PMID:14559226</ref>
-{{STRUCTURE_1wkn|  PDB=1wkn  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===A PLAUSIBLE MODEL OF FULL-LENGTH INTEGRASEDNA COMPLEX===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_14559226}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:014559226</ref><references group="xtra"/>
 [[Category: Barreca, M L]]
 [[Category: Chimirri, A]]