(Q27641919)

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Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein

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Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein (English)

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crystal structure

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1 reference

based on heuristic

inferred from title

Christian Cambillau

4

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5

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Jean-Marie Bourhis

2

object named as

Jean-Marie Bourhis

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6

object named as

Sonia Longhi

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Kenth Johansson

1

object named as

Kenth Johansson

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author name string

Valerie Campanacci

3

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language of work or name

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publication date

7 November 2003

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Journal of Biological Chemistry

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278

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45

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44567-73

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Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures

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Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association

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Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures

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Significant differences in nucleocapsid morphology within the Paramyxoviridae

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The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein

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Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

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Separate domains of Sendai virus P protein are required for binding to viral nucleocapsids

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The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles

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Reexamination of the Sendai virus P protein domains required for RNA synthesis: a possible supplemental role for the P protein

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The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

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Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration

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The relationship of conformational changes in the sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide

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Protein interaction domains of the measles virus nucleocapsid protein (NP).

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Domains of the measles virus N protein required for binding to P protein and self-assembly

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Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself

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The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins

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Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils

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Deletion analysis defines a carboxyl-proximal region of Sendai virus P protein that binds to the polymerase L protein

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Protein interactions entered into by the measles virus P, V, and C proteins

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Tetrameric coiled coil domain of Sendai virus phosphoprotein

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Assignment of the 1H, 15N and 13C resonances of the nucleocapsid-binding domain of the Sendai virus phosphoprotein.

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Preparation of selenomethionyl proteins for phase determination

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Identifiers

10.1074/JBC.M308745200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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