3eyf: Difference between revisions
New page: '''Unreleased structure''' The entry 3eyf is ON HOLD Authors: Thomson, C.A., Bryson, S., McLean, G.R., Creagh, A.L., Pai, E.F., Schrader, J.W. Description: Germline V-genes sculpt the ... |
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==Crystal structure of anti-human cytomegalovirus antibody 8f9 plus gB peptide== | |||
<StructureSection load='3eyf' size='340' side='right'caption='[[3eyf]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3eyf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_Towne Human herpesvirus 5 strain Towne]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EYF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=3eyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eyf OCA], [https://pdbe.org/3eyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eyf RCSB], [https://www.ebi.ac.uk/pdbsum/3eyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eyf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6PJF2_HUMAN Q6PJF2_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Immunoglobulin genes are generated somatically through specialized mechanisms resulting in a vast repertoire of antigen-binding sites. Despite the stochastic nature of these processes, the V-genes that encode most of the antigen-combining site are under positive evolutionary selection, raising the possibility that V-genes have been selected to encode key structural features of binding sites of protective antibodies against certain pathogens. Human, neutralizing antibodies to human cytomegalovirus that bind the AD-2S1 epitope on its gB envelope protein repeatedly use a pair of well-conserved, germline V-genes IGHV3-30 and IGKV3-11. Here, we present crystallographic, kinetic and thermodynamic analyses of the binding site of such an antibody and that of its primary immunoglobulin ancestor. These show that these germline V-genes encode key side chain contacts with the viral antigen and thereby dictate key structural features of the hypermutated, high-affinity neutralizing antibody. V-genes may thus encode an innate, protective immunological memory that targets vulnerable, invariant sites on multiple pathogens. | |||
Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus.,Thomson CA, Bryson S, McLean GR, Creagh AL, Pai EF, Schrader JW EMBO J. 2008 Oct 8;27(19):2592-602. Epub 2008 Sep 4. PMID:18772881<ref>PMID:18772881</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3eyf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Human herpesvirus 5 strain Towne]] | |||
[[Category: Large Structures]] | |||
[[Category: Bryson S]] | |||
[[Category: Creagh AL]] | |||
[[Category: McLean GR]] | |||
[[Category: Pai EF]] | |||
[[Category: Schrader JW]] | |||
[[Category: Thomson CA]] | |||
Latest revision as of 09:37, 6 September 2023
Crystal structure of anti-human cytomegalovirus antibody 8f9 plus gB peptideCrystal structure of anti-human cytomegalovirus antibody 8f9 plus gB peptide
Structural highlights
FunctionPublication Abstract from PubMedImmunoglobulin genes are generated somatically through specialized mechanisms resulting in a vast repertoire of antigen-binding sites. Despite the stochastic nature of these processes, the V-genes that encode most of the antigen-combining site are under positive evolutionary selection, raising the possibility that V-genes have been selected to encode key structural features of binding sites of protective antibodies against certain pathogens. Human, neutralizing antibodies to human cytomegalovirus that bind the AD-2S1 epitope on its gB envelope protein repeatedly use a pair of well-conserved, germline V-genes IGHV3-30 and IGKV3-11. Here, we present crystallographic, kinetic and thermodynamic analyses of the binding site of such an antibody and that of its primary immunoglobulin ancestor. These show that these germline V-genes encode key side chain contacts with the viral antigen and thereby dictate key structural features of the hypermutated, high-affinity neutralizing antibody. V-genes may thus encode an innate, protective immunological memory that targets vulnerable, invariant sites on multiple pathogens. Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus.,Thomson CA, Bryson S, McLean GR, Creagh AL, Pai EF, Schrader JW EMBO J. 2008 Oct 8;27(19):2592-602. Epub 2008 Sep 4. PMID:18772881[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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