5igx: Difference between revisions
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f7e|5f7e]], [[5fa2|5fa2]], [[5fec|5fec]], [[5i9q|5i9q]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f7e|5f7e]], [[5fa2|5fa2]], [[5fec|5fec]], [[5i9q|5i9q]]</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=5igx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5igx OCA], [http://pdbe.org/5igx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5igx RCSB], [http://www.ebi.ac.uk/pdbsum/5igx PDBsum]</span></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=5igx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5igx OCA], [http://pdbe.org/5igx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5igx RCSB], [http://www.ebi.ac.uk/pdbsum/5igx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5igx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 13:16, 27 September 2017
Crystal structure of NIH45-46 Fab germline precursor in complex with 426c.TM1deltaV1-3 gp120Crystal structure of NIH45-46 Fab germline precursor in complex with 426c.TM1deltaV1-3 gp120
Structural highlights
Publication Abstract from PubMedEfforts to elicit broadly neutralizing antibodies (bNAbs) against HIV-1 require understanding germline bNAb recognition of HIV-1 envelope glycoprotein (Env). The VRC01-class bNAb family derived from the VH1-2*02 germline allele arose in multiple HIV-1-infected donors, yet targets the CD4-binding site on Env with common interactions. Modified forms of the 426c Env that activate germline-reverted B cell receptors are candidate immunogens for eliciting VRC01-class bNAbs. We present structures of germline-reverted VRC01-class bNAbs alone and complexed with 426c-based gp120 immunogens. Germline bNAb-426c gp120 complexes showed preservation of VRC01-class signature residues and gp120 contacts, but detectably different binding modes compared to mature bNAb-gp120 complexes. Unlike typical antibody-antigen interactions, VRC01-class germline antibodies exhibited preformed antigen-binding conformations for recognizing immunogens. Affinity maturation introduced substitutions increasing induced-fit recognition and electropositivity, potentially to accommodate negatively-charged complex-type N-glycans on gp120. These results provide general principles relevant to the unusual evolution of VRC01-class bNAbs and guidelines for structure-based immunogen design. Structural basis for germline antibody recognition of HIV-1 immunogens.,Scharf L, West AP, Sievers SA, Chen C, Jiang S, Gao H, Gray MD, McGuire AT, Scheid JF, Nussenzweig MC, Stamatatos L, Bjorkman PJ Elife. 2016 Mar 21;5. pii: e13783. doi: 10.7554/eLife.13783. PMID:26997349[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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