BAIT

PROPEP1

ARABIDOPSIS THALIANA PEPTIDE 1, ATPEP1, MXK3.13, MXK3_13, PEP1, PEPTIDE 1, precursor of peptide 1, AT5G64900
precursor of peptide 1
GO Process (4)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

PEPR1

ATPEPR1, F3N23.28, F3N23_28, PEP1 RECEPTOR 1, AT1G73080
leucine-rich repeat receptor-like protein kinase PEPR1
Arabidopsis thaliana (Columbia)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1.

Tang J, Han Z, Sun Y, Zhang H, Gong X, Chai J

The endogenous peptides AtPep1-8 in Arabidopsis mature from the conserved C-terminal portions of their precursor proteins PROPEP1-8, respectively. The two homologous leucine-rich repeat-receptor kinases (LRR-RKs) PEPR1 and PEPR2 act as receptors of AtPeps. AtPep binding leads to stable association of PEPR1,2 with the shared receptor LRR-RK BAK1, eliciting immune responses similar to those induced by pathogens. Here we report a ... [more]

Cell Res. Jan. 01, 2015; 25(1);110-20 [Pubmed: 25475059]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PEPR1 PROPEP1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
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Curated By

  • BioGRID