2005
DOI: 10.1110/ps.051411805
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The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

Abstract: Measles virus is a negative-sense, single-stranded RNA virus within the Mononegavirales order, which includes several human pathogens, including rabies, Ebola, Nipah, and Hendra viruses. The measles virus nucleoprotein consists of a structured N-terminal domain, and of an intrinsically disordered C-terminal domain, N TAIL (aa 401-525), which undergoes induced folding in the presence of the C-terminal domain (XD, aa 459-507) of the viral phosphoprotein. Within N TAIL , an a-helical molecular recognition element… Show more

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Cited by 138 publications
(258 citation statements)
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References 81 publications
(134 reference statements)
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“…In this latter case, indeed, our previous SPR and fluorescence spectroscopy studies indicated a K D in the 100 nM range (46), contrary to ITC and SPR studies carried out by Kingston and colleagues (98,126) that revealed a K D of 7.4 -13 M. It should be noted however that these latter studies were carried out using N TAIL peptides encompassing residues 477-505 or 477-525 rather than full-length N TAIL (98,126).…”
Section: Structural Models Of Henipavirus N Tail -P Xd Complexes and contrasting
confidence: 70%
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“…In this latter case, indeed, our previous SPR and fluorescence spectroscopy studies indicated a K D in the 100 nM range (46), contrary to ITC and SPR studies carried out by Kingston and colleagues (98,126) that revealed a K D of 7.4 -13 M. It should be noted however that these latter studies were carried out using N TAIL peptides encompassing residues 477-505 or 477-525 rather than full-length N TAIL (98,126).…”
Section: Structural Models Of Henipavirus N Tail -P Xd Complexes and contrasting
confidence: 70%
“…Using the same approach, we showed that both NiV and HeV N TAIL undergo ␣-helical induced folding upon binding to the corresponding P X domain. Binding of Henipavirus N TAIL domains to P XD results in the same type of structural transitions as observed with the MeV N TAIL -P XD couple (6,44,46) and is in agreement with the strong ␣-helical propensity of Henipavirus N TAIL (14). Note however that these studies remain qualitative; if the estimated ␣-helical content is useful for comparative purposes, deconvolution approaches notoriously lead to estimations that cannot be taken as fully reliable, i.e.…”
Section: The X Domains Of Henipavirus P Proteins Bind To the Intrinsisupporting
confidence: 69%
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“…Indeed, the C-terminal domain of the nucleoprotein (N tail ) of measles virus, which is involved in a number important functions, is intrinsically unstructured. [22][23][24][25] Metal-thiolate clusters-Several proteins known as metallothioneins rely on metal-thiolate clusters in their functions. There are at least ten known closely related metallothionein proteins expressed in humans.…”
Section: Ligands Interacting With Intrinsically Disordered Proteinsmentioning
confidence: 99%