Measles Virus Nucleoprotein
Seiten
2007
Nova Science Publishers Inc (Verlag)
978-1-60021-629-9 (ISBN)
Nova Science Publishers Inc (Verlag)
978-1-60021-629-9 (ISBN)
Measles virus possesses a non segmented, single stranded, negative sense RNA genome that is encapsidated by the nucleoprotein to form a helical nucleocapsid. This book focuses on the structural information available on the nucleoprotein, showing that it consists of a structured core (NCORE) and of a disordered C-terminal domain (NTAIL).
Measles virus possesses a non segmented, single stranded, negative sense RNA genome that is encapsidated by the nucleoprotein to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNAdependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein. This book focuses on the main structural information available on the nucleoprotein, showing that it consists of a structured core (NCORE) and of an intrinsically disordered C-terminal domain (NTAIL). The functional implications of the disordered nature of NTAIL are discussed in light of the ability of disordered regions to establish interactions with multiple partners, thus leading to multiple biological effects. Indeed, beyond the phosphoprotein, NTAIL also interacts with cellular partners, including the major heat shock protein, hsp72, the interferon regulator factor 3, IRF3, and a yet unidentified cellular receptor referred to as NR. This book consists of two chapters devoted to the general functions of the nucleoprotein in transcription and replication and to a detailed overview of its structural properties, and of three chapters focused on the functional relevance of the interaction between NTAIL and its various intracellular and extracellular partners.
Measles virus possesses a non segmented, single stranded, negative sense RNA genome that is encapsidated by the nucleoprotein to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNAdependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein. This book focuses on the main structural information available on the nucleoprotein, showing that it consists of a structured core (NCORE) and of an intrinsically disordered C-terminal domain (NTAIL). The functional implications of the disordered nature of NTAIL are discussed in light of the ability of disordered regions to establish interactions with multiple partners, thus leading to multiple biological effects. Indeed, beyond the phosphoprotein, NTAIL also interacts with cellular partners, including the major heat shock protein, hsp72, the interferon regulator factor 3, IRF3, and a yet unidentified cellular receptor referred to as NR. This book consists of two chapters devoted to the general functions of the nucleoprotein in transcription and replication and to a detailed overview of its structural properties, and of three chapters focused on the functional relevance of the interaction between NTAIL and its various intracellular and extracellular partners.
Preface; Structural Organisation and Functional Role of the Intrinsically Disordered C-terminal Domain; Measles Virus Nucleocapsid Structure, Conformational Flexibility and the Rule of Six; Nucleocapsid Protein Interactions with the major inducible 70 kDa Heat Shock Protein; Interferon Regulator Factor 3 as Cellular Partner of Measles Virus Nucleoprotein; Interaction of Measles Virus Nucleoprotein with Cell Surface Receptors: Impact on Cell Biology and Immune Response; Index.
| Erscheint lt. Verlag | 20.2.2007 |
|---|---|
| Zusatzinfo | Illustrations |
| Verlagsort | New York |
| Sprache | englisch |
| Maße | 260 x 180 mm |
| Gewicht | 542 g |
| Themenwelt | Medizin / Pharmazie ► Medizinische Fachgebiete ► Mikrobiologie / Infektologie / Reisemedizin |
| ISBN-10 | 1-60021-629-3 / 1600216293 |
| ISBN-13 | 978-1-60021-629-9 / 9781600216299 |
| Zustand | Neuware |
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