| First appeared in release:||Release 2.0 (02/14/2005)|
|SwissProt: ||NCAP_MEASE |
|TrEMBL: || |
|NCBI (GI): ||127900 |
|Source organism:||Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus)|
10 20 30 40 50 60
| | | | | |
MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLIG - 60
NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPDVSIR LLEVVQSDQS QSGLTFASRG - 120
TNMEDEADQY FSHDDPSSSD QSRSGWFENK EISDIEVQDP EGFNMILGTI LAQIWVLLAK - 180
AVTAPDTAAD SELRRWIKYT QQRRVVGEFR LERKWLDVVR NRIAEDLSLR RFMVALILDI - 240
KRTPGNKPRI AEMICDIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTLESLM - 300
NLYQQMGETA PYMVILENSI QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA - 360
YFRLGQEMVR RSAGKVSSTL ASELGITAED ARLVSEIAMH TTEDRISRAV GPRQAQVSFL - 420
HGDQSENELP GLGGKEDRRV KQGRGEARES YRETGSSRAS DARAAHPPTS MPLDIDTASE - 480
SGQDPQDSRR SADALLRLQA MAGILEEQGS DTDTPRVYND RDLLD
|Functional narrative |
The Measles virus nucleocapsid protein is comprised of an N-terminal domain, NCORE, which is resistant to proteolysis and a C-terminal domain, NTAIL, which is hypersensitive to proteolysis. The nucleoprotein, in complex with its physiological partner phosphoprotein and RNA polymerase, packages the viral RNA genome. Its disorder promoting sequence, spectroscopic and hydrodynamic properties indicate that the NTAIL belongs to the pre-molten globule family.
|Map of ordered and disordered regions|
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|Type:||Disordered - Pre-Molten Globule|
|Location:||401 - 525|
|Modification type: ||Engineered |
|PDB: || |
|Structural/functional type: ||Function arises via a disorder to order transition |
|Functional classes: ||Molecular recognition effectors |
|Functional subclasses: ||Protein-protein binding |
|Detection methods: |
- Nuclear magnetic resonance (NMR) (pH: 7; protein 0.5 mM; sodium phosphate 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; sodium phosphate 10 mM; TFE (increasing concentrations (0,10,20,30)) 30 %)
- Small-angle X-ray scattering (SAXS) (281 K; EDTA (buffer) 5 mM; glycerol (radiation scavenger) 10 %; Tris/HCl (buffer) 10 mM)
- Dynamic light scattering (pH: 7; sodium phosphate 10 mM)
- Dynamic light scattering (pH: 8; NaCl (concentrated at 1.25mg/ml.) 75 mM; Tris/HCl 10 mM)
- Size exclusion/gel filtration chromatography
- Sensitivity to proteolysis (N tail (purified) 1 ug; SDS-PAGE 12 %; trypsin 0.25 ug)
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
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)
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).
The part of the N-tail region undergoing alpha-helical induced folding: aa 488-505. Johansson et al. (2003); Bourhis et al. (2004).
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).
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).
The part of the N-tail region involved in binding to Hsp72: aa 488-505 and 517-525. Zhang et al. (2005).
- 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).
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.
[AV 08/06/2010 Longhi, S.]
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