Trans-homophilic interaction of PECAM-1

Stable Identifier
R-HSA-210285
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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
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
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
Participants
Participant Of
Orthologous Events
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Created