Structural modeling of a plant disease resistance gene product domain

Citation
Dj. Rigden et al., Structural modeling of a plant disease resistance gene product domain, PROTEINS, 41(1), 2000, pp. 133-143
Citations number
84
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEINS-STRUCTURE FUNCTION AND GENETICS
ISSN journal
08873585 → ACNP
Volume
41
Issue
1
Year of publication
2000
Pages
133 - 143
Database
ISI
SICI code
0887-3585(20001001)41:1<133:SMOAPD>2.0.ZU;2-K
Abstract
Dominant plant resistance genes are involved in the protection of plants ag ainst a wide variety of pathogens. Sequence analysis has revealed a variety of classes, often having domains in common. One commonly found region has come to be known as a putative nucleotide-binding site (NBS) due to the sim ple presence of sequence motifs. Until now, no experimental evidence has su pported this idea. Here we suggest, as an alternative hypothesis, that part of this region is structurally homologous to the receiver domain common to many proteins of His-Asp phosphotransfer pathways. This conclusion is base d on sequence analysis, threading experiments, and the construction of a mo lecular model of one domain that performs well against structure validation tools. The new hypothesis, in contrast to the NBS hypothesis, can explain the devastating effect of a Thr-->Ala mutation in a well-characterized resi stance gene product. According to the new hypothesis, regions located N-ter minal and C-terminal to the modeled portion, containing highly conserved se quence motifs, could form a separate domain. Proteins 2000;41:133-143. (C) 2000 Wiley-Liss, Inc.