3o6l: Difference between revisions
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<StructureSection load='3o6l' size='340' side='right'caption='[[3o6l]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3o6l' size='340' side='right'caption='[[3o6l]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o6l]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3o6l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O6L FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o6l OCA], [https://pdbe.org/3o6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o6l RCSB], [https://www.ebi.ac.uk/pdbsum/3o6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o6l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q98XH7_9HIV1 Q98XH7_9HIV1] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human immunodeficiency virus 1]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Gouet | [[Category: Gouet P]] | ||
[[Category: Guillon | [[Category: Guillon C]] | ||
[[Category: Serriere | [[Category: Serriere J]] | ||
Latest revision as of 12:29, 6 September 2023
Anti-Tat HIV 11H6H1 Fab' complexed with a 15-mer Tat peptideAnti-Tat HIV 11H6H1 Fab' complexed with a 15-mer Tat peptide
Structural highlights
FunctionPublication Abstract from PubMedTat, the transcriptional activator protein of human immunodeficiency virus type 1 (HIV-1), is critical for viral replication and is a potential HIV-1 vaccine candidate. This intrinsically disordered protein is present in the extracellular medium and is involved in the pathogenicity of HIV through its interaction with different cellular and viral biological partners. A monoclonal antibody termed 11H6H1, which is specific for the N-terminal region of Tat, was selected for a functional and structural study of the HIV-1 Tat protein. The equilibrium dissociation constants (K(d)) of Tat and Tat fragments complexed with 11H6H1 were estimated by competitive ELISA. Tat contains a single tryptophan residue, Trp11, located in the N-terminal region. We show that the substitution of Trp11 by a phenylalanine completely abolishes the binding of 11H6H1, whereas the transactivating activity of Tat is preserved. The epitope recognized by 11H6H1 was restricted to the 9-mer peptide P(6)KLEPWKHP(14) centered on Trp11. The crystal structures of this 9-mer peptide and of an overlapping 15-mer peptide were determined in complex with Fab' 11H6H1 at 2.4 A and 2.1 A resolution, respectively. Tat is intrinsically disordered and can undergo induced folding upon association with a biological partner. Our crystallographic study reveals that the two Tat peptides, which are lodged in the U-shaped groove of the Fab' antigen-binding site, adopt a standard type I beta-turn conformation. The central Trp11 that is critical for Fab' recognition is further stabilized by pi-stacking interactions. The structural and biological consequences of this induced folding in HIV pathogenesis are discussed. Fab'-Induced Folding of Antigenic N-Terminal Peptides from Intrinsically Disordered HIV-1 Tat Revealed by X-ray Crystallography.,Serriere J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C J Mol Biol. 2010 Oct 28. PMID:21035463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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