Abstract
Many flowering plants possess a self-incompatibility system to prevent inbreeding. In Brassica rapa, self/non-self recognition in mating is established through S-haplotype-specific interactions between stigma receptors and S-locus protein 11 (SP11, also called S-locus cysteine-rich protein) that is encoded at the highly polymorphic S-locus. Here we describe the solution structure of the SP11 protein of the S8-haplotype (S 8-SP11), which specifically binds to the stigma factor of the same haplotype. It folds into an α/β sandwich structure that resembles those of plant defensins. Residues important for structural integrity are highly conserved among the allelic SP11s, suggesting the existence of a common folding pattern. Structure-based sequence alignment and homology modeling of allelic SP11 identified a hypervariable (HV) region, which is thought to form a loop that bulges out from the body of the protein that is amenable to solvent exposure. We suggest that the HV region could serve as a specific binding site for the stigma receptor.
Original language | English |
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Pages (from-to) | 36389-36395 |
Number of pages | 7 |
Journal | Journal of Biological Chemistry |
Volume | 278 |
Issue number | 38 |
DOIs | |
State | Published - 19 Sep 2003 |