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PMID:19275899

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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

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

MEASF:NCAP

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P03422

F

Seeded From UniProt


Notes

See also

References

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