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PDBsum entry 1jrf
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protein metals links
Signaling protein, membrane protein PDB id
1jrf

 

 

 

 

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Contents
Protein chain
47 a.a. *
Metals
_CA
* Residue conservation analysis
PDB id:
1jrf
Name: Signaling protein, membrane protein
Title: Nmr solution structure of the viral receptor domain of tva
Structure: Subgroup a rous sarcoma virus receptors pg800 and pg950. Chain: a. Fragment: ldl-a domain. Synonym: tva ldl-a module. Low density lipoprotein receptor-related protein. Engineered: yes
Source: Coturnix japonica. Japanese quail. Organism_taxid: 93934. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 20 models
Authors: Q.-Y.Wang,W.Huang,K.Dolmer,P.G.W.Gettins,L.Rong
Key ref: Q.Y.Wang et al. (2002). Solution structure of the viral receptor domain of Tva and its implications in viral entry. J Virol, 76, 2848-2856. PubMed id: 11861852
Date:
13-Aug-01     Release date:   08-Mar-02    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P98162  (RSVR_COTJA) -  Subgroup A Rous sarcoma virus receptor pg950 from Coturnix japonica
Seq:
Struc: 		157 a.a.
47 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
J Virol 76:2848-2856 (2002)
PubMed id: 11861852  
 
 
Solution structure of the viral receptor domain of Tva and its implications in viral entry.
Q.Y.Wang, W.Huang, K.Dolmer, P.G.Gettins, L.Rong.
 
  ABSTRACT  
 
Tva is the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A). The viral receptor function of Tva is determined by a 40-residue, cysteine-rich motif called the LDL-A module. Here we report the solution structure of the LDL-A module of Tva, determined by nuclear magnetic resonance (NMR) spectroscopy. Although the carboxyl terminus of the Tva LDL-A module has a structure similar to those of other reported LDL-A modules, the amino terminus adopts a different conformation. The LDL-A module of Tva does not contain the signature antiparallel beta-sheet observed in other LDL-A modules, and it is more flexible than other reported LDL-A modules. The LDL-A structure of Tva provides mechanistic insights into how a simple viral receptor functions in retrovirus entry. The side chains of H38 and W48 of Tva, which have been identified as viral contact residues by mutational analysis, are solvent exposed, suggesting that they are directly involved in EnvA binding. However, the side chain of L34, another potential viral contact residue identified previously, is buried inside of the module and forms the hydrophobic core with other residues. Thus L34 likely stabilizes the Tva structure but is not a viral interaction determinant. In addition, we propose that the flexible amino-terminal region of Tva plays an important role in determining specificity in the Tva-EnvA interaction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20218331 T.Miyazawa (2009).
[Receptors for animal retroviruses].
  Uirusu, 59, 223-242.  
15952897 H.Jeon, and S.C.Blacklow (2005).
Structure and physiologic function of the low-density lipoprotein receptor.
  Annu Rev Biochem, 74, 535-562.  
15950875 N.Beglova, and S.C.Blacklow (2005).
The LDL receptor: how acid pulls the trigger.
  Trends Biochem Sci, 30, 309-317.  
15731243 S.E.Delos, J.A.Godby, and J.M.White (2005).
Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.
  J Virol, 79, 3488-3499.  
16282473 S.Nizet, J.Wruss, N.Landstetter, L.Snyers, and D.Blaas (2005).
A mutation in the first ligand-binding repeat of the human very-low-density lipoprotein receptor results in high-affinity binding of the single V1 module to human rhinovirus 2.
  J Virol, 79, 14730-14736.  
16282495 T.Rai, M.Caffrey, and L.Rong (2005).
Identification of two residues within the LDL-A module of Tva that dictate the altered receptor specificity of mutant subgroup A avian sarcoma and leukosis viruses.
  J Virol, 79, 14962-14966.  
15564460 D.Elleder, D.C.Melder, K.Trejbalova, J.Svoboda, and M.J.Federspiel (2004).
Two different molecular defects in the Tva receptor gene explain the resistance of two tvar lines of chickens to infection by subgroup A avian sarcoma and leukosis viruses.
  J Virol, 78, 13489-13500.  
14722295 J.G.Smith, W.Mothes, S.C.Blacklow, and J.M.Cunningham (2004).
The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection.
  J Virol, 78, 1403-1410.  
14694099 T.Rai, D.Marble, K.Rihani, and L.Rong (2004).
The spacing between cysteines two and three of the LDL-A module of Tva is important for subgroup A avian sarcoma and leukosis virus entry.
  J Virol, 78, 683-691.  
12805452 X.Yu, Q.Y.Wang, Y.Guo, K.Dolmer, J.A.Young, P.G.Gettins, and L.Rong (2003).
Kinetic analysis of binding interaction between the subgroup A Rous sarcoma virus glycoprotein SU and its cognate receptor Tva: calcium is not required for ligand binding.
  J Virol, 77, 7517-7526.  
12381843 Q.Y.Wang, B.Manicassamy, X.Yu, K.Dolmer, P.G.Gettins, and L.Rong (2002).
Characterization of the LDL-A module mutants of Tva, the subgroup A Rous sarcoma virus receptor, and the implications in protein folding.
  Protein Sci, 11, 2596-2605.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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