SSF48345

A virus capsid protein alpha-helical domain

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR008935

The capsid of spherical viruses is built from a limited number of proteins and often displays icosahedral symmetry. Rotaviruses have a segmented double-stranded RNA genome enclosed in a complex capsid formed by three concentric protein layers. The proteins forming the capsid are VP2 (internal layer, with triangulation T = 1 and an asymmetric dimer in the icosahedral repeating unit), VP6 (intermediate layer, T = 13 symmetry), VP7 (external layer, T = 13) and VP4, which forms a spike inserted in the outermost two layers. The major capsid protein VP6 self-assembles into spherical or helical particles mainly depending upon pH. VP6 assemblies arise from different pickings of a unique dimer of trimers. The repeating unit of the helix contains a pair of trimers related by a radial dyad
[1]
. The VP6 trimer is composed of two domains: a head (external) and a base (internal), leaving a central cavity, these are formed by a distal β-barrel domain and a proximal α-helical domain, which interact with the outer and inner layer of the virion, respectively
[2]
.

References
Imported from IPR008935

1.Structural polymorphism of the major capsid protein of rotavirus. Lepault J, Petitpas I, Erk I, Navaza J, Bigot D, Dona M, Vachette P, Cohen J, Rey FA. EMBO J. 20, 1498-507, (2001). View articlePMID: 11285214

2.Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion. Mathieu M, Petitpas I, Navaza J, Lepault J, Kohli E, Pothier P, Prasad BV, Cohen J, Rey FA. EMBO J. 20, 1485-97, (2001). View articlePMID: 11285213

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