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PMID:19275899
Citation |
Bernard, C, Gely, S, Bourhis, JM, Morelli, X, Longhi, S and Darbon, H (2009) Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR. FEBS Lett. 583:1084-9 |
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Abstract |
In this paper we investigate the interaction between the C-terminal domains of the measles virus phosphoprotein (XD) and nucleoprotein (N(TAIL)) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both N(TAIL) constructs and peptides, we show that contrary to the conserved Box2 region (N(489-506)), the C-terminal region of N(TAIL) (N(513-525)) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of N(TAIL) would stabilize the N(TAIL)-XD complex either via a functional coupling with N(489-506) or by reducing the entropic penalty associated to the binding-coupled-to-folding process. |
Links |
PubMed Online version:10.1016/j.febslet.2009.03.004 |
Keywords |
Measles virus/chemistry; Measles virus/metabolism; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Nucleocapsid Proteins/chemistry; Nucleocapsid Proteins/metabolism; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Protein Folding; Protein Structure, Tertiary/physiology; Viral Proteins/chemistry; Viral Proteins/metabolism |
Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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enables |
GO:0005515: protein binding |
ECO:0000353: physical interaction evidence used in manual assertion |
UniProtKB:P03422 |
F |
Seeded From UniProt |
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Notes
See also
References
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