7n07: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n07 OCA], [https://pdbe.org/7n07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n07 RCSB], [https://www.ebi.ac.uk/pdbsum/7n07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n07 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n07 OCA], [https://pdbe.org/7n07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n07 RCSB], [https://www.ebi.ac.uk/pdbsum/7n07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n07 ProSAT]</span></td></tr> | ||
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<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The early humoral immune response to acute HIV-1 infection is largely non-neutralizing. The principal target of these antibodies is the primary immunodominant region (PID) on the gp41 fusion protein. The PID is a highly conserved 15-residue region displayed on the surface of HIV-1 virions. In this study, we analyzed the humoral determinants of HIV-1 gp41 PID binding using biophysical, structural, and computational methods. In complex with a patient-derived near-germline antibody fragment, the PID motif adopts an elongated random coil, whereas the PID bound to affinity-matured Fab adopts a strand-turn-helix conformation. Molecular dynamics simulations showed that the PID is structurally plastic suggesting that the PID can form an ensemble of structural states recognized by various non-neutralizing antibodies, facilitating HIV-1 immunodominance observed in acute and chronic HIV-1 infections. An improved understanding of how the HIV-1 gp41 PID misdirects the early humoral response should guide the development of an effective HIV-1 vaccine. | |||
Conformational plasticity of the HIV-1 gp41 immunodominant region is recognized by multiple non-neutralizing antibodies.,Cook JD, Khondker A, Lee JE Commun Biol. 2022 Mar 31;5(1):291. doi: 10.1038/s42003-022-03235-w. PMID:35361878<ref>PMID:35361878</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 7n07" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 16:44, 6 November 2024
Crystal structure of the apo 3D6 antibody fragmentCrystal structure of the apo 3D6 antibody fragment
Structural highlights
Publication Abstract from PubMedThe early humoral immune response to acute HIV-1 infection is largely non-neutralizing. The principal target of these antibodies is the primary immunodominant region (PID) on the gp41 fusion protein. The PID is a highly conserved 15-residue region displayed on the surface of HIV-1 virions. In this study, we analyzed the humoral determinants of HIV-1 gp41 PID binding using biophysical, structural, and computational methods. In complex with a patient-derived near-germline antibody fragment, the PID motif adopts an elongated random coil, whereas the PID bound to affinity-matured Fab adopts a strand-turn-helix conformation. Molecular dynamics simulations showed that the PID is structurally plastic suggesting that the PID can form an ensemble of structural states recognized by various non-neutralizing antibodies, facilitating HIV-1 immunodominance observed in acute and chronic HIV-1 infections. An improved understanding of how the HIV-1 gp41 PID misdirects the early humoral response should guide the development of an effective HIV-1 vaccine. Conformational plasticity of the HIV-1 gp41 immunodominant region is recognized by multiple non-neutralizing antibodies.,Cook JD, Khondker A, Lee JE Commun Biol. 2022 Mar 31;5(1):291. doi: 10.1038/s42003-022-03235-w. PMID:35361878[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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