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.

Publication

Structural insight into the specific interaction between murine SHPS-1/SIRP alpha and its ligand CD47.

Nakaishi A, Hirose M, Yoshimura M, Oneyama C, Saito K, Kuki N, Matsuda M, Honma N, Ohnishi H, Matozaki T, Okada M, Nakagawa A

SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1 (SHPS-1 or SIRP alpha/BIT) is an immunoglobulin (Ig) superfamily transmembrane receptor and a member of the signal regulatory protein (SIRP) family involved in cell-cell interaction. SHPS-1 binds to its ligand CD47 to relay an inhibitory signal for cellular responses, whereas SIRPbeta, an activating member of the same family, does not bind ... [more]

J. Mol. Biol. Jan. 18, 2008; 375(3);650-60 [Pubmed: 18045614]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

SIRPA

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]protein phosphorylated amino acid binding [IPI]

Gene Ontology Cellular Component