2K9D
Solution structure of the domain X of measle phosphoprotein
Summary for 2K9D
Entry DOI | 10.2210/pdb2k9d/pdb |
Descriptor | Phosphoprotein (1 entity in total) |
Functional Keywords | measle, morbillivirus, phosphoprotein, x domain, rna editing, rna replication, viral protein |
Biological source | Measles virus |
Total number of polymer chains | 1 |
Total formula weight | 5169.16 |
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 citation | Bernard, 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: 19275899DOI: 10.1016/j.febslet.2009.03.004 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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