Source:http://www.reactome.org/biopax/48887BiochemicalReaction1263
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Authored: Garapati, P V, 2008-07-30 10:22:58,
Edited: Garapati, P V, 2008-07-30 10:22:58,
Interaction with ERM may lead to lateral oligomerization of phosphorylated L1 and this enhances the homophilic trans adhesion of L1.<br>L1 mediates cell-cell adhesion by a trans-homophilic binding mechanism. In the nonengaged resting state the L1 N-terminal Ig domains adopt a horseshoe like structure due to an intramolecular binding between domains 1 and 4 or 2 and 3, respectively. When engaged in homophilic binding between adjacent cells, L1 could undergo a conformational change leading to a pairwise antiparallel alignment of Ig domains 1-4 and 2-3.<br>,
Reviewed: Maness, PF, 2010-02-16
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http://identifiers.org/pubmed/17538021,
http://identifiers.org/pubmed/19278660,
http://identifiers.org/pubmed/2448316,
http://identifiers.org/pubmed/7493978,
http://identifiers.org/pubmed/9721721,
urn:biopax:UnificationXref:REACTOME DATABASE ID_374680,
urn:biopax:UnificationXref:REACTOME_REACT_22211_1
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L1 trans-homophilic interaction
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