TTEDRISRAVGPRQAQVSFLHGDQSENELPGLGGKEDRRVKQGRGEARESYRETGSSRAS
DARAAHPPTSMPLDIDTASESGQDPQDSRRSADALLRLQAMAGILEEQGSDTDTPRVYND
RDLLD

1. Nuclear magnetic resonance (NMR) (pH: 7; protein 0.5 mM; sodium phosphate 10 mM)


2. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; sodium phosphate 10 mM; TFE (increasing concentrations (0,10,20,30)) 30 %)


3. Small-angle X-ray scattering (SAXS) (281 K; EDTA (buffer) 5 mM; glycerol (radiation scavenger) 10 %; Tris/HCl (buffer) 10 mM)


4. Dynamic light scattering (pH: 7; sodium phosphate 10 mM)


5. Dynamic light scattering (pH: 8; NaCl (concentrated at 1.25mg/ml.) 75 mM; Tris/HCl 10 mM)


6. Size exclusion/gel filtration chromatography


7. Sensitivity to proteolysis (N tail (purified) 1 ug; SDS-PAGE 12 %; trypsin 0.25 ug)

1. Bourhis JM, Johansson K, Receveur-Brechot V, Oldfield CJ, Dunker KA, Canard B, Longhi S. "The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner." Virus Res. 2004; 99(2): 157-67. PubMed: 14749181
   
   
2. Bourhis JM, Receveur-Brechot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. "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." Protein Sci. 2005; 14(8): 1975-92. PubMed: 16046624
   
   
3. Buckland R, Gerald C, Barker D, Wild F. "Cloning and sequencing of the nucleoprotein gene of measles virus (Hallé strain)." Nucleic Acids Res. 1988; 16(24): 11821. PubMed: 3211755
   
   
4. Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. "Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein." J Mol Recognit. 2010. PubMed: 20058326
   
   
5. Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S. "Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein." J Biol Chem. 2003; 278(45): 44567-73. PubMed: 12944395
   
   
6. Laine D, Bourhis JM, Longhi S, Flacher M, Cassard L, Canard B, Sautès-Fridman C, Rabourdin-Combe C, Valentin H. "Measles virus nucleoprotein induces cell-proliferation arrest and apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions, respectively." J. Gen. Virol.. 2005; 86(Pt 6): 1771-84. PubMed: 15914856
   
   
7. Laine D, Trescol-Biemont MC, Longhi S, Libeau G, Marie JC, Vidalain PO, Azocar O, Diallo A, Canard B, Rabourdin-Combe C, Valentin H. "Measles virus (MV) nucleoprotein binds to a novel cell surface receptor distinct from FcgammaRII via its C-terminal domain: role in MV-induced immunosuppression." J Virol. 2003; 77(21): 11332-11346. PubMed: 14557619
   
   
8. Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. "The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein." J Biol Chem. 2003; 278(20): 18638-18648. PubMed: 12621042
   
   
9. Zhang X, Bourhis JM, Longhi S, Carsillo T, Buccellato M, Morin B, Canard B, Oglesbee M. "Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus." Virology. 2005; 337(1): 162-74. PubMed: 15914229
   
   

The experimental NTAIL sequence in the Longhi et al. (2003) article contained four additional amino acids plus a 6X Histidine tag fused to the N-terminus of amino acids 399-523 of the SwissProt sequence. The experimental sequence was obtained through direct correspondence with Longhi. The secondary structure predictor, JPRED, predicts an alpha-helix at amino acids 489-504.

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The Gely et al. (2010), paper offers NMR evidence of a gain in alpha-helical structure for aa 490-504, and for structural transitions of NTAIL induced by interaction with the nucleocapsid-binding domain (XD, aa 459-507) of Phosphoprotein. (See DP00133: MeV Phosphoprotein)

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The N-tail region belongs to the premolten globule subfamily and shows alpha-helical propensity (as seen by CD studies with TFE). Longhi et al. (2003).

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The part of the N-tail region undergoing alpha-helical induced folding: aa 488-505. Johansson et al. (2003); Bourhis et al. (2004).

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The parts of the N-tail region involved in binding to the C-terminal domain of P (X domain, aa 457-507): aa 488-505 and 517-525. Bourhis et al. (2005). See DP00133 for MeV Phosphoprotein (aka protein P).

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The part of the N-tail region involved in binding to the extracellular nuceloprotein receptor NR: aa 401-420. Laine et al. (2003); Laine et al. (2005).

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The part of the N-tail region involved in binding to Hsp72: aa 488-505 and 517-525. Zhang et al. (2005).

1. Takeuchi K, Miyajima N, Kobune F, Tashiro M. "Comparative nucleotide sequence analyses of the entire genomes of B95a cell-isolated and vero cell-isolated measles viruses from the same patient." Virus Genes. 2000; 20(3): 253-7. PubMed: 10949953
   
   

The native sequence used in DP00160 is from UniProt ID (unreviewed): Q784S3 (Q784S3_9PARA); Takeuchi, et al. (2000) PMID 10949953. A reviewed UniProt entry with slight sequence variations exists at P04851 (NCAP_MEASE).

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Additional references for Protein P (DP00133) and Protein N (DP00160): Belle et al. Proteins. 2008 Dec;73(4):973-88. PMID: 18536007; Bernard et al. FEBS Lett. 2009 Apr 2;583(7):1084-9. Epub 2009 Mar 9. PMID: 19275899; Couturier et al. J Mol Recognit. 2010 May;23(3):301-15. PMID: 19718689; Kavalenka et al. Biophys J. 2010 Mar 17;98(6):1055-64. PMID: 20303863; Longhi, Oglesbee. Protein Pept Lett. 2010;17(8):961-78. PMID: 20450481; Longhi. Curr Top Microbiol Immunol. 2009;329:103-28. Review. PMID: 19198564; Morin et al. J Phys Chem B. 2006 Oct 19;110(41):20596-608. PMID: 17034249.

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[AV 08/06/2010 Longhi, S.]