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
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.