3eyf: Difference between revisions

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[[Image:3eyf.png|left|200px]]


{{STRUCTURE_3eyf| PDB=3eyf | SCENE= }}
==Crystal structure of anti-human cytomegalovirus antibody 8f9 plus gB peptide==
<StructureSection load='3eyf' size='340' side='right'caption='[[3eyf]], [[Resolution|resolution]] 2.30&Aring;' 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]] 2.3&#8491;</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.


===Crystal structure of anti-human cytomegalovirus antibody 8f9 plus gB peptide===
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>


{{ABSTRACT_PUBMED_18772881}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3eyf" style="background-color:#fffaf0;"></div>
[[3eyf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EYF OCA].


==See Also==
==See Also==
*[[Antibody|Antibody]]
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[3D structures of human antibody|3D structures of human antibody]]
==Reference==
== References ==
<ref group="xtra">PMID:018772881</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bryson, S.]]
[[Category: Human herpesvirus 5 strain Towne]]
[[Category: Creagh, A L.]]
[[Category: Large Structures]]
[[Category: McLean, G R.]]
[[Category: Bryson S]]
[[Category: Pai, E F.]]
[[Category: Creagh AL]]
[[Category: Schrader, J W.]]
[[Category: McLean GR]]
[[Category: Thomson, C A.]]
[[Category: Pai EF]]
[[Category: Antibody]]
[[Category: Schrader JW]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Thomson CA]]
[[Category: Cytomegalovirus]]
[[Category: Envelope protein]]
[[Category: Glycoprotein]]
[[Category: Host-virus interaction]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Membrane]]
[[Category: Transmembrane]]
[[Category: Virion]]

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

3eyf is a 6 chain structure with sequence from Homo sapiens and Human herpesvirus 5 strain Towne. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6PJF2_HUMAN

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Thomson CA, Bryson S, McLean GR, Creagh AL, Pai EF, Schrader JW. Germline V-genes sculpt the binding site of a family of antibodies neutralizing human cytomegalovirus. EMBO J. 2008 Oct 8;27(19):2592-602. Epub 2008 Sep 4. PMID:18772881 doi:10.1038/emboj.2008.179

3eyf, resolution 2.30Å

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