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2K9D

Solution structure of the domain X of measle phosphoprotein

Summary for 2K9D
Entry DOI10.2210/pdb2k9d/pdb
DescriptorPhosphoprotein (1 entity in total)
Functional Keywordsmeasle, morbillivirus, phosphoprotein, x domain, rna editing, rna replication, viral protein
Biological sourceMeasles virus
Total number of polymer chains1
Total formula weight5169.16
Authors
Gely, S.,Bernard, C.,Bourhis, J.M.,Longhi, S.,Darbon, H. (deposition date: 2008-10-08, release date: 2009-10-20, Last modification date: 2024-05-29)
Primary citationBernard, C.,Gely, S.,Bourhis, J.M.,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., 583:1084-1089, 2009
Cited by
PubMed 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.
PubMed: 19275899
DOI: 10.1016/j.febslet.2009.03.004
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-18公开中

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