1qiu
From Proteopedia
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A TRIPLE BETA-SPIRAL IN THE ADENOVIRUS FIBRE SHAFT REVEALS A NEW STRUCTURAL MOTIF FOR BIOLOGICAL FIBRES
Overview
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.
About this Structure
1QIU is a Single protein structure of sequence from Human adenovirus 2. Full crystallographic information is available from OCA.
Reference
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
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