2015
DOI: 10.1128/jvi.01612-15
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A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of Human Respiratory Syncytial Virus

Abstract: Presently, respiratory syncytial virus (RSV), the main cause of severe respiratory infections in infants, cannot be treated efficiently with antivirals. However, its RNA-dependent polymerase complex offers potential targets for RSV-specific drugs. This includes the recognition of its template, the ribonucleoprotein complex (RNP), consisting of genomic RNA encapsidated by the RSV nucleoprotein, N. This recognition proceeds via interaction between the phosphoprotein P, which is the main polymerase cofactor, and … Show more

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Cited by 59 publications
(90 citation statements)
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“…4C). By fitting the CSP data with a two-site fast exchange model, a K d of 25-50 M was determined, in agreement with a K d of 30 M previously determined for the N NTD ⅐P CD complex by isothermal titration calorimetry (39).…”
Section: Extent Of Intrinsically Disordered Regions In Hrsv Phossupporting
confidence: 81%
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“…4C). By fitting the CSP data with a two-site fast exchange model, a K d of 25-50 M was determined, in agreement with a K d of 30 M previously determined for the N NTD ⅐P CD complex by isothermal titration calorimetry (39).…”
Section: Extent Of Intrinsically Disordered Regions In Hrsv Phossupporting
confidence: 81%
“…4C). Surprisingly, no signal was recovered for the very C-terminal Phe 241 residue, which in X-ray structures appears to be the main structural determinant for NC⅐P complex formation, by tightly inserting into a hydrophobic pocket at the surface of N NTD (39). Our results thus suggest the possibility of additional binding modes corresponding to weaker interactions.…”
Section: Extent Of Intrinsically Disordered Regions In Hrsv Phosmentioning
confidence: 64%
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