3eyf: Difference between revisions

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<StructureSection load='3eyf' size='340' side='right'caption='[[3eyf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3eyf' size='340' side='right'caption='[[3eyf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3eyf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eyo|3eyo]], [[3eyq|3eyq]], [[3f12|3f12]]</div></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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GB_HCMVT GB_HCMVT]] Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that likely serve as postattachment entry receptors. Participates also in the fusion of viral and cellular membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL (By similarity).  Viral ligand for CD209/DC-SIGN. This interaction allows capture of viral particles by dendritic (DCs) cells and subsequent virus transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. CMV subverts the migration properties of dendritic cells to gain access to target organs or susceptible cells.
[https://www.uniprot.org/uniprot/Q6PJF2_HUMAN Q6PJF2_HUMAN]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Human herpesvirus 5 strain Towne]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bryson, S]]
[[Category: Bryson S]]
[[Category: Creagh, A L]]
[[Category: Creagh AL]]
[[Category: McLean, G R]]
[[Category: McLean GR]]
[[Category: Pai, E F]]
[[Category: Pai EF]]
[[Category: Schrader, J W]]
[[Category: Schrader JW]]
[[Category: Thomson, C A]]
[[Category: Thomson CA]]
[[Category: Antibody]]
[[Category: Cleavage on pair of basic residue]]
[[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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