4xc1: Difference between revisions
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''' | ==Crystal structure of human 4E10 Fab in complex with its peptide epitope on HIV-1 GP41: crystals cryoprotected with sn-Glycerol 3-phosphate== | ||
<StructureSection load='4xc1' size='340' side='right' caption='[[4xc1]], [[Resolution|resolution]] 1.63Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xc1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XC1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G3P:SN-GLYCEROL-3-PHOSPHATE'>G3P</scene>, <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=41H:(BETAS)-BETA-METHYL-L-PHENYLALANINE'>41H</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xaw|4xaw]], [[4xbg|4xbg]], [[4xbe|4xbe]], [[4xc3|4xc3]], [[4xbp|4xbp]], [[4xce|4xce]], [[4xcc|4xcc]], [[4xcf|4xcf]], [[4xcn|4xcn]], [[4xcy|4xcy]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xc1 OCA], [http://pdbe.org/4xc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xc1 RCSB], [http://www.ebi.ac.uk/pdbsum/4xc1 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Numerous studies of the anti-HIV-1 envelope glycoprotein 41 (gp41) broadly neutralizing antibody 4E10 suggest that 4E10 also interacts with membrane lipids, but the antibody regions contacting lipids and its orientation with respect to the viral membrane are unknown. Vaccine immunogens capable of re-eliciting these membrane proximal external region (MPER)-like antibodies may require a lipid component to be successful. We performed a systematic crystallographic study of lipid binding to 4E10 to identify lipids bound by the antibody and the lipid-interacting regions. We identified phosphatidic acid, phosphatidylglycerol, and glycerol phosphate as specific ligands for 4E10 in the crystal structures. 4E10 used its CDRH1 loop to bind the lipid head groups, while its CDRH3 interacted with the hydrophobic lipid tails. Identification of the lipid binding sites on 4E10 may aid design of immunogens for vaccines that include a lipid component in addition to the MPER on gp41 for generation of broadly neutralizing antibodies. | |||
Crystallographic Identification of Lipid as an Integral Component of the Epitope of HIV Broadly Neutralizing Antibody 4E10.,Irimia A, Sarkar A, Stanfield RL, Wilson IA Immunity. 2016 Jan 19;44(1):21-31. doi: 10.1016/j.immuni.2015.12.001. Epub 2016, Jan 5. PMID:26777395<ref>PMID:26777395</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xc1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Irimia, A]] | [[Category: Irimia, A]] | ||
[[Category: Stanfield, R L]] | |||
[[Category: Wilson, I A]] | |||
[[Category: 4e10 fab]] | |||
[[Category: Hiv-1 gp41 mper]] | |||
[[Category: Immune system]] | |||
[[Category: Lipid membrane]] | |||
Revision as of 18:46, 3 February 2016
Crystal structure of human 4E10 Fab in complex with its peptide epitope on HIV-1 GP41: crystals cryoprotected with sn-Glycerol 3-phosphateCrystal structure of human 4E10 Fab in complex with its peptide epitope on HIV-1 GP41: crystals cryoprotected with sn-Glycerol 3-phosphate
Structural highlights
Publication Abstract from PubMedNumerous studies of the anti-HIV-1 envelope glycoprotein 41 (gp41) broadly neutralizing antibody 4E10 suggest that 4E10 also interacts with membrane lipids, but the antibody regions contacting lipids and its orientation with respect to the viral membrane are unknown. Vaccine immunogens capable of re-eliciting these membrane proximal external region (MPER)-like antibodies may require a lipid component to be successful. We performed a systematic crystallographic study of lipid binding to 4E10 to identify lipids bound by the antibody and the lipid-interacting regions. We identified phosphatidic acid, phosphatidylglycerol, and glycerol phosphate as specific ligands for 4E10 in the crystal structures. 4E10 used its CDRH1 loop to bind the lipid head groups, while its CDRH3 interacted with the hydrophobic lipid tails. Identification of the lipid binding sites on 4E10 may aid design of immunogens for vaccines that include a lipid component in addition to the MPER on gp41 for generation of broadly neutralizing antibodies. Crystallographic Identification of Lipid as an Integral Component of the Epitope of HIV Broadly Neutralizing Antibody 4E10.,Irimia A, Sarkar A, Stanfield RL, Wilson IA Immunity. 2016 Jan 19;44(1):21-31. doi: 10.1016/j.immuni.2015.12.001. Epub 2016, Jan 5. PMID:26777395[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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