5f7e: Difference between revisions

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<StructureSection load='5f7e' size='340' side='right'caption='[[5f7e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5f7e' size='340' side='right'caption='[[5f7e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5f7e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7E FirstGlance]. <br>
<table><tr><td colspan='2'>[[5f7e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F7E FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fa2|5fa2]], [[5fec|5fec]], [[5i9q|5i9q]], [[5igx|5igx]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=5f7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7e OCA], [http://pdbe.org/5f7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f7e RCSB], [http://www.ebi.ac.uk/pdbsum/5f7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7e 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=5f7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7e OCA], [https://pdbe.org/5f7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f7e RCSB], [https://www.ebi.ac.uk/pdbsum/5f7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7e ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bjorkman, P J]]
[[Category: Bjorkman PJ]]
[[Category: Jiang, S]]
[[Category: Jiang S]]
[[Category: Scharf, L]]
[[Category: Scharf L]]
[[Category: Sievers, S A]]
[[Category: Sievers SA]]
[[Category: Antibody]]
[[Category: Hiv-1]]
[[Category: Immune system]]

Latest revision as of 09:41, 19 July 2023

Crystal structure of germ-line precursor of 3BNC60 FabCrystal structure of germ-line precursor of 3BNC60 Fab

Structural highlights

5f7e is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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.

See Also

References

  1. Scharf L, West AP, Sievers SA, Chen C, Jiang S, Gao H, Gray MD, McGuire AT, Scheid JF, Nussenzweig MC, Stamatatos L, Bjorkman PJ. Structural basis for germline antibody recognition of HIV-1 immunogens. Elife. 2016 Mar 21;5. pii: e13783. doi: 10.7554/eLife.13783. PMID:26997349 doi:http://dx.doi.org/10.7554/eLife.13783

5f7e, resolution 1.90Å

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OCA