5fec: Difference between revisions

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-'''Unreleased structure'''
-The entry 5fec is ON HOLD
+==Crystal structure of 3BNC60 Fab germline precursor in complex with 426c.TM4deltaV1-3 gp120==
+<StructureSection load='5fec' size='340' side='right' caption='[[5fec]], [[Resolution|resolution]] 3.17&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5fec]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FEC FirstGlance]. <br>
+</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5fec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fec OCA], [http://pdbe.org/5fec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fec RCSB], [http://www.ebi.ac.uk/pdbsum/5fec PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Efforts 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.
-Authors: Scharf, L., Bjorkman, P.J.
+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<ref>PMID:26997349</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Bjorkman, P.J]]
+<div class="pdbe-citations 5fec" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bjorkman, P J]]
 [[Category: Scharf, L]]
+[[Category: Antibody]]
+[[Category: Hiv-1]]
+[[Category: Immune system]]