Trans-homophilic interaction of PECAM-1

Stable Identifier
R-HSA-210285
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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

Buckley, CD, Simmons, DL, Harvey, DJ, Newton, JP, Hunter, AP

Biochem Biophys Res Commun 1999
9252369 Residues on both faces of the first immunoglobulin fold contribute to homophilic binding sites of PECAM-1/CD31

Buckley, CD, Jones, EY, Simmons, DL, Newton, JP

J Biol Chem 1997
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