| General information | | DisProt: | DP00133 | | Name: | Phosphoprotein | | Synonym(s): | PHOSP_MEASE
Protein P
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P03422 | | UniGene: | | | SwissProt: | PHOSP_MEASE | | TrEMBL: | | | NCBI (GI): | 133668 | | Source organism: | Measles virus (strain Edmonston) (Subacute sclerose panencephalitis virus) | | Sequence length: | 507 | | Percent disordered: | 62% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MAEEQARHVK NGLECIRALK AEPIGSLAIE EAMAAWSEIS DNPGQERATC REEKAGSSGL - 60
SKPCLSAIGS TEGGAPRIRG QGPGESDDDA ETLGIPPRNL QASSTGLQCY YVYDHSGEAV - 120
KGIQDADSIM VQSGLDGDST LSGGDNESEN SDVDIGEPDT EGYAITDRGS APISMGFRAS - 180
DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSGTPIKK GTERRLASFG - 240
TEIASLLTGG ATQCARKSPS EPSGPGAPAG NVPECVSNAA LIQEWTPESG TTISPRSQNN - 300
EEGGDYYDDE LFSDVQDIKT ALAKIHEDNQ KIISKLESLL LLKGEVESIK KQINRQNISI - 360
STLEGHLSSI MIAIPGLGKD PNDPTADVEI NPDLKPIIGR DSGRALAEVL KKPVASRQLQ - 420
GMTNGRTSSR GQLLKEFQLK PIGKKMSSAV GFVPDTGPAS RSVIRSIIKS SRLEEDRKRY - 480
LMTLLDDIKG ANDLAKFHQM LMKIIMK
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| Functional narrative |
"Measles virus (MV), a member of the family Paramyxoviridae,
is a major human pathogen, responsible annually
for more than 1 million deaths worldwide.... MV is an enveloped virus with a nonsegmented, singlestranded,
negative RNA genome. The genomic RNA is
packaged by the nucleoprotein (N) to form the viral nucleocapsid.
Transcription and replication are carried out
on this (N:RNA) complex by the polymerase L in association
with the phosphoprotein P.... P and N each perform
several functions during the viral cycle. Both transcription
and replication take place onto the assembled form
of N (NNUC), but the replication step also necessitates the
concomitant assembly of the soluble, unassembled form
of N (N°) onto the newly synthesized viral genomic RNA,
with the participation of P. At least in the case of MV , N°
undergoes a conformational maturation before being encapsidated.... P plays a pivotal role
together with N in the transition from transcription to
replication. P is a modular protein with two distinct functional
domains. The P C-terminal
domain (PCT), which is the most conserved in
sequence, contains all the regions required for viral
transcription. On the other hand, the poorly conserved
N-terminal domain (PNT) provides several additional
functions required for replication." (Karlin et al. 2002)
|
| 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.
|
| Region 1 | | Type: | Disordered | | Name: | PNT | | Location: | 1 - 230 | | Length: | 230 | | Region sequence: |
MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGL
SKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAV
KGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRAS
DVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKK | | Modification type: | Engineered
Fragment
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; 10 mM sodium phosphate buffer; 1-mm-thick quartz cells)
- Sensitivity to proteolysis (298 K; pH: 7.8; 1 mg/ml protein in 20 mM Tris/HCl ; Horse heart cytochrome c (type VI) and thermolysin; protease:protein substrate ratio 1:100)
- Dynamic light scattering (293 K; pH: 8; 1 mg/ml protein in 100 mM NaCl)
- Size exclusion/gel filtration chromatography (pH: 7; 100 mM NaCl; 50 mM sodium phosphate buffer; Superdex 200 column)
- Nuclear magnetic resonance (NMR) (300 K; pH: 5.6; 0.3 mM protein; 30 mM NaCl; 50 mM sodium acetate)
| References:
- Karlin D, Longhi S, Receveur V, Canard B. "The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins." Virology. 2002; 296(2): 251-62. PubMed: 12069524
| Comments:Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906.
|
| Region 3 | | Type: | Disordered | | Name: | linker | | Location: | 376 - 458 | | Length: | 83 | | Region sequence: |
GLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLK
EFQLKPIGKKMSSAVGFVPDTGP | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Sensitivity to proteolysis
| References:
There are no documents referencing this region. | Comments:Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906.
The main reference for Region 3: Longhi et al. (2003) PMID 12621042. See overall References section below for complete record.
|
| Region 4 | | Type: | Disordered | | Name: | Flexible loop of the nucleocapsid-binding domain (XD) | | Location: | 489 - 491 | | Length: | 3 | | Region sequence: |
KGA | | Modification type: | Fragment
Monomeric
| | PDB: | 1OKS:A, 1T6O:A, 2K9D:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (300 K; pH: 8; 1.6mM in 10mM sodium phosphate, 10%D(2)O)
| References:
- 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
| Comments:This flexible loop is part of an ordered domain, the extreme C-terminal domain (XD) (aa 459-507). XD also serves as the nucleocapsid-binding domain. The 3D solution structure of XD consists of three alpha helices (aa 462-470, 475-487 and 492-505), a turn between helices 1 and 2 (aa 471-474) and a highly dynamic flexible turn (aa 488-491).
Additional reference regarding the modular organization of DP133 'Protein P': Karlin et al., J Gen Virol. 2003 Dec;84(Pt 12):3239-52., PMID 14645906.
|
| References |
- 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
- Karlin D, Ferron F, Canard B, Longhi S. "Structural disorder and modular organization in Paramyxovirinae N and P." 2003; 84(Pt 12): 3239-52. PubMed: 14645906
- 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
- Parks CL, Lerch RA, Walpita P, Wang HP, Sidhu MS, Udem SA. "Comparison of predicted amino acid sequences of measles virus strains in the Edmonston vaccine lineage." J Virol. 2001; 75(2): 910-20. PubMed: 11134304
|
| Comments |
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.
Sent for [AV
Longhi S.]
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