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PDBsum entry 1w71

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protein Protein-protein interface(s) links
Disease resistance PDB id
1w71

 

 

 

 

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Contents
Protein chains
132 a.a.
Theoretical model
PDB id:
1w71
Name: Disease resistance
Title: Theoretical model of the three-dimensional structure of a disease resistance gene homolog encoding resistance protein from vigna mungo
Structure: Vigna mungo yellow mosaic virus resistance 1. Chain: a, b. Fragment: nb-arc domain, residues 1-132
Source: Vigna mungo. Blackgram
Authors: J.Basak,R.P.Bahadur,A.Pal,C.Mukhopadhyay
Key ref: J.Basak and R.P.Bahadur (2006). Theoretical model of the three-dimensional structure of a disease resistance gene homolog encoding resistance protein in Vigna mungo. J Biomol Struct Dyn, 24, 123-130. PubMed id: 16928135
Date:
24-Aug-04     Release date:   22-Feb-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7XZT9  (Q7XZT9_VIGRA) -  Viral resistance candidate (Fragment)
Seq:
Struc:
129 a.a.
132 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 9 residue positions (black crosses)

 

 
J Biomol Struct Dyn 24:123-130 (2006)
PubMed id: 16928135  
 
 
Theoretical model of the three-dimensional structure of a disease resistance gene homolog encoding resistance protein in Vigna mungo.
J.Basak, R.P.Bahadur.
 
  ABSTRACT  
 
Plant disease resistance (R) genes, the key players of innate immunity system in plants encode 'R' proteins. 'R' protein recognizes product of avirulance gene from the pathogen and activate downstream signaling responses leading to disease resistance. No three dimensional (3D) structural information of any 'R' proteins is available as yet. We have reported a 'R' gene homolog, the 'VMYR1', encoding 'R' protein in Vigna mungo. Here, we describe the homology modeling of the 'VMYR1' protein. The model was created by using the 3D structure of an ATP-binding cassette transporter protein from Vibrio cholerae as a template. The strategy for homology modeling was based on the high structural conservation in the superfamily of P-loop containing nucleoside triphosphate hydrolase in which target and template proteins belong. This is the first report of theoretical model structure of any 'R' proteins.
 

 

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