3uzq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3uzq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_1 Dengue virus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UZQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3uzq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_1 Dengue virus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UZQ FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uyp|3uyp]], [[3uze|3uze]], [[3uzv|3uzv]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uyp|3uyp]], [[3uze|3uze]], [[3uzv|3uzv]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uzq RCSB], [http://www.ebi.ac.uk/pdbsum/3uzq PDBsum]</span></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=3uzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uzq RCSB], [http://www.ebi.ac.uk/pdbsum/3uzq PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q9II01_9FLAV Q9II01_9FLAV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody.,Cockburn JJ, Navarro Sanchez ME, Fretes N, Urvoas A, Staropoli I, Kikuti CM, Coffey LL, Arenzana Seisdedos F, Bedouelle H, Rey FA Structure. 2012 Feb 8;20(2):303-14. Epub 2012 Jan 26. PMID:22285214<ref>PMID:22285214</ref>
Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody.,Cockburn JJ, Navarro Sanchez ME, Fretes N, Urvoas A, Staropoli I, Kikuti CM, Coffey LL, Arenzana Seisdedos F, Bedouelle H, Rey FA Structure. 2012 Feb 8;20(2):303-14. Epub 2012 Jan 26. PMID:22285214<ref>PMID:22285214</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
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[[Category: Dengue virus 1]]
[[Category: Dengue virus 1]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Bedouelle, H.]]
[[Category: Bedouelle, H]]
[[Category: Cockburn, J J.B.]]
[[Category: Cockburn, J J.B]]
[[Category: Coffey, L L.]]
[[Category: Coffey, L L]]
[[Category: Fretes, N.]]
[[Category: Fretes, N]]
[[Category: Kikuti, C M.]]
[[Category: Kikuti, C M]]
[[Category: Rey, F A.]]
[[Category: Rey, F A]]
[[Category: Sanchez, M E.Navarro.]]
[[Category: Sanchez, M E.Navarro]]
[[Category: Seisdedos, F Arenzana.]]
[[Category: Seisdedos, F Arenzana]]
[[Category: Staropoli, I.]]
[[Category: Staropoli, I]]
[[Category: Urvoas, A.]]
[[Category: Urvoas, A]]
[[Category: Dengue antibody neutralization]]
[[Category: Dengue antibody neutralization]]
[[Category: Immune system]]
[[Category: Immune system]]

Revision as of 10:33, 25 December 2014

Crystal structure of the dengue virus serotype 1 envelope protein domain III in complex with the variable domains of Mab 4E11Crystal structure of the dengue virus serotype 1 envelope protein domain III in complex with the variable domains of Mab 4E11

Structural highlights

3uzq is a 2 chain structure with sequence from Dengue virus 1 and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[Q9II01_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]

Publication Abstract from PubMed

The dengue virus (DENV) complex is composed of four distinct but serologically related flaviviruses, which together cause the present-day most important emerging viral disease. Although DENV infection induces lifelong immunity against viruses of the same serotype, the antibodies raised appear to contribute to severe disease in cases of heterotypic infections. Understanding the mechanisms of DENV neutralization by antibodies is, therefore, crucial for the design of vaccines that simultaneously protect against all four viruses. Here, we report a comparative, high-resolution crystallographic analysis of an "A-strand" murine monoclonal antibody, Mab 4E11, in complex with its target domain of the envelope protein from the four DENVs. Mab 4E11 is capable of neutralizing all four serotypes, and our study reveals the determinants of this cross-reactivity. The structures also highlight the mechanism by which A-strand Mabs disrupt the architecture of the mature virion, inducing premature fusion loop exposure and concomitant particle inactivation.

Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody.,Cockburn JJ, Navarro Sanchez ME, Fretes N, Urvoas A, Staropoli I, Kikuti CM, Coffey LL, Arenzana Seisdedos F, Bedouelle H, Rey FA Structure. 2012 Feb 8;20(2):303-14. Epub 2012 Jan 26. PMID:22285214[1]

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

References

  1. Cockburn JJ, Navarro Sanchez ME, Fretes N, Urvoas A, Staropoli I, Kikuti CM, Coffey LL, Arenzana Seisdedos F, Bedouelle H, Rey FA. Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody. Structure. 2012 Feb 8;20(2):303-14. Epub 2012 Jan 26. PMID:22285214 doi:http://dx.doi.org/10.1016/j.str.2012.01.001

3uzq, resolution 1.60Å

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