Structural highlights
Function
[PHOSP_MEASE] Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR.,Bernard C, Gely S, Bourhis JM, Morelli X, Longhi S, Darbon H FEBS Lett. 2009 Apr 2;583(7):1084-9. Epub 2009 Mar 9. PMID:19275899[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernard C, Gely S, Bourhis JM, Morelli X, Longhi S, Darbon H. Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR. FEBS Lett. 2009 Apr 2;583(7):1084-9. Epub 2009 Mar 9. PMID:19275899 doi:10.1016/j.febslet.2009.03.004