1qiu

From Proteopedia

(Difference between revisions)

Revision as of 07:15, 17 January 2018

A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for biological fibres

Structural highlights

1qiu is a 6 chain structure with sequence from Ade02. The December 2010 RCSB PDB Molecule of the Month feature on Adenovirus by David Goodsell is 10.2210/rcsb_pdb/mom_2010_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1qhv
Gene:	LOCUS AD2H2 (ADE02)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPIKE_ADE02] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blocking the cell-cell adhesion function of CXADR dimers and leading to local disruption of the tight junction. Fiber protein present on neo-synthesized particles may thus disrupt the junctional integrity in order to facilitate further neighboring cells infection. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Fiber shedding is dependent on viral CXADR drifting motion and subsequent binding to immobile integrins. Heparan sulfate might also play a role in virus binding.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human adenoviruses are responsible for respiratory, gastroenteric and ocular infections and can serve as gene therapy vectors. They form icosahedral particles with 240 copies of the trimeric hexon protein arranged on the planes and a penton complex at each of the twelve vertices. The penton consists of a pentameric base, implicated in virus internalization, and a protruding trimeric fibre, responsible for receptor attachment. The fibres are homo-trimeric proteins containing an amino-terminal penton base attachment domain, a long, thin central shaft and a carboxy-terminal cell attachment or head domain. The shaft domain contains a repeating sequence motif with an invariant glycine or proline and a conserved pattern of hydrophobic residues. Here we describe the crystal structure at 2.4 A resolution of a recombinant protein containing the four distal repeats of the adenovirus type 2 fibre shaft plus the receptor-binding head domain. The structure reveals a novel triple beta-spiral fibrous fold for the shaft. Implications for folding of fibrous proteins (misfolding of shaft peptides leads to amyloid-like fibrils) and for the design of a new class of artificial, silk-like fibrous materials are discussed.

A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein.,van Raaij MJ, Mitraki A, Lavigne G, Cusack S Nature. 1999 Oct 28;401(6756):935-8. PMID:10553913^[5]

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

References

↑ Dechecchi MC, Tamanini A, Bonizzato A, Cabrini G. Heparan sulfate glycosaminoglycans are involved in adenovirus type 5 and 2-host cell interactions. Virology. 2000 Mar 15;268(2):382-90. PMID:10704346 doi:http://dx.doi.org/10.1006/viro.1999.0171
↑ Walters RW, Freimuth P, Moninger TO, Ganske I, Zabner J, Welsh MJ. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell. 2002 Sep 20;110(6):789-99. PMID:12297051
↑ Burckhardt CJ, Suomalainen M, Schoenenberger P, Boucke K, Hemmi S, Greber UF. Drifting motions of the adenovirus receptor CAR and immobile integrins initiate virus uncoating and membrane lytic protein exposure. Cell Host Microbe. 2011 Aug 18;10(2):105-17. doi: 10.1016/j.chom.2011.07.006. PMID:21843868 doi:http://dx.doi.org/10.1016/j.chom.2011.07.006
↑ Wang K, Huang S, Kapoor-Munshi A, Nemerow G. Adenovirus internalization and infection require dynamin. J Virol. 1998 Apr;72(4):3455-8. PMID:9525681
↑ van Raaij MJ, Mitraki A, Lavigne G, Cusack S. A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature. 1999 Oct 28;401(6756):935-8. PMID:10553913 doi:10.1038/44880

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qiu"

@@ Line 1: / Line 1: @@
-==A TRIPLE BETA-SPIRAL IN THE ADENOVIRUS FIBRE SHAFT REVEALS A NEW STRUCTURAL MOTIF FOR BIOLOGICAL FIBRES==
+==A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for biological fibres==
 <StructureSection load='1qiu' size='340' side='right' caption='[[1qiu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qhv|1qhv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LOCUS AD2H2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10515 ADE02])</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=1qiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qiu OCA], [http://pdbe.org/1qiu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qiu RCSB], [http://www.ebi.ac.uk/pdbsum/1qiu 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=1qiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qiu OCA], [http://pdbe.org/1qiu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qiu RCSB], [http://www.ebi.ac.uk/pdbsum/1qiu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qiu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/1qiu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/1qiu_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 38: / Line 39: @@
 [[Category: Lavigne, G]]
 [[Category: Mitraki, A]]
-[[Category: Raaij, M J.Van]]
+[[Category: Raaij, M J.van]]
 [[Category: Fibre protein]]
 [[Category: Triple beta-spiral]]

1qiu

From Proteopedia

Revision as of 07:15, 17 January 2018

A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for biological fibres

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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