Reactome | Trans-homophilic interaction of PECAM-1

Trans-homophilic interaction of PECAM-1

Stable Identifier

R-HSA-210285

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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PECAM-mediated adhesion is complex, because it is capable of binding both to itself (homophilic adhesion) and to non-PECAM ligands (heterophilic adhesion). The trans-homophilic interaction between the two PECAM-1 molecules is mediated by their NH2-terminal membrane distal Ig homology domains 1 and 2 plus the proper spacing formed by the six Ig-homology domains.

Literature References

PubMed ID	Title	Journal	Year
10425179	CD31 (PECAM-1) exists as a dimer and is heavily N-glycosylated Newton, JP, Hunter, AP, Simmons, DL, Buckley, CD, Harvey, DJ	Biochem Biophys Res Commun	1999
9252369	Residues on both faces of the first immunoglobulin fold contribute to homophilic binding sites of PECAM-1/CD31 Newton, JP, Buckley, CD, Jones, EY, Simmons, DL	J Biol Chem	1997