Functional Role of Structural Disorder in Capsid Proteins

Liljas, Lars

doi:10.1002/9781118135570.ch2

Cited by 3 publications

(2 citation statements)

References 34 publications

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“…A significant portion of the CPs of both nonenveloped and enveloped spherical (+)-strand RNA viruses are structurally flexible. In addition to being difficult to resolve in crystallographic structures, they are likely to be intrinsically disordered (Ivanyi-Nagy et al, 2008;Liljas, 2011). Intrinsically disordered sequences are typically characterized by a high proportion of polar and charged residues and underrepresentation of bulky hydrophobic residues.…”

Section: Structurally Flexible Regions In the Cpmentioning

confidence: 99%

Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses

Kao

2013

Virology

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Viral capsid proteins (CPs) are characterized by their role in forming protective shells around viral genomes. However, CPs have additional and important roles in the virus infection cycles and in the cellular response to infection. These activities involve CP binding to RNAs in both sequence-specific and nonspecific manners as well as association with other proteins. This review focuses on CPs of both plant and animal-infecting viruses with positive-strand RNA genomes. We summarize the structural features of CPs and describe their modulatory roles in viral translation, RNA-dependent RNA synthesis, and host defense responses.

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Section: Structurally Flexible Regions In the Cpmentioning

confidence: 99%

Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses

Kao

2013

Virology

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“…Disordered regions of capsid proteins, commonly known as arms, do not simply play crucial structural roles, but are highly involved in a wide range of biological functions. This idea is reinforced by the excellent reviews by Liljas, , who analyzed and systemized the functional repertoire of various viral capsid proteins and revealed that viral disordered arms can interact with nucleic acids, are involved in the control of the capsid assembly and disassembly, and, obviously, play a crucial role in the stabilization of the assembled capsid structure.…”

Section: Intrinsic Disorder In Structural Proteinsmentioning

confidence: 99%

Structural Disorder in Viral Proteins

Xue¹,

et al. 2014

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Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein

Kordyukova

Shtykova

Baratova

et al. 2018

Journal of Biomolecular Structure and Dynamics

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Influenza A virus, a member of the Orthomyxoviridae family of enveloped viruses, is one of the human and animal top killers, and its structure and components are therefore extensively studied during the last decades. The most abundant component, M1 matrix protein, forms a matrix layer (scaffold) under the viral lipid envelope, and the functional roles as well as structural peculiarities of the M1 protein are still under heavy debate. Despite multiple attempts of crystallization, no high resolution structure is available for the full length M1 of Influenza A virus. The likely reason for the difficulties lies in the intrinsic disorder of the M1 C-terminal part preventing diffraction quality crystals to be grown. Alternative structural methods including synchrotron small-angle X-ray scattering (SAXS), atomic force microscopy, cryo-electron microscopy/tomography are therefore widely applied to understand the structure of M1, its self-association and interactions with the lipid membrane and the viral nucleocapsid. These methods reveal striking similarities in the behavior of M1 and matrix proteins of other enveloped RNA viruses, with the differences accompanied by the specific features of the viral lifecycles, thus suggesting common interaction principles and, possibly, common evolutional ancestors. The structural information on the Influenza A virus M1 protein obtained to the date strongly suggests that the intrinsic disorder in the C-terminal domain has important functional implications.

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Functional Role of Structural Disorder in Capsid Proteins

Cited by 3 publications

References 34 publications

Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses

Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses

Structural Disorder in Viral Proteins

Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein

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