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From Proteopedia
A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for biological fibres
Structural highlights
FunctionSPIKE_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 PubMedHuman 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
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