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Details on Person Interaction with ERM may lead to lateral oligomerization of ...

Class:IdSummation:374622
_displayNameInteraction with ERM may lead to lateral oligomerization of ...
_timestamp2009-12-30 21:52:25
created[InstanceEdit:374621] Garapati, P V, 2008-07-30 10:18:31
literatureReference[LiteratureReference:443576] Fast turnover of L1 adhesions in neuronal growth cones involving both surface diffusion and exo/endocytosis of L1 molecules
[LiteratureReference:443579] Identification of a homophilic binding site in immunoglobulin-like domain 2 of the cell adhesion molecule L1
modified[InstanceEdit:390358] Garapati, P V, 2009-01-30 00:00:17
[InstanceEdit:443578] Garapati, P V, 2009-10-12
[InstanceEdit:443805] Garapati, P V, 2009-10-12
[InstanceEdit:444909] Garapati, P V, 2009-10-27
[InstanceEdit:447049] Garapati, P V, 2009-11-19
[InstanceEdit:451256] Garapati, P V, 2009-12-30
textInteraction with ERM may lead to lateral oligomerization of phosphorylated L1 and this enhances the homophilic trans adhesion of L1.
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.
(summation)[Reaction:374680] L1 trans-homophilic interaction [Homo sapiens]
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