3m45: Difference between revisions
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{{STRUCTURE_3m45| PDB=3m45 | SCENE= }} | {{STRUCTURE_3m45| PDB=3m45 | SCENE= }} | ||
===Crystal structure of Ig1 domain of mouse SynCAM 2=== | ===Crystal structure of Ig1 domain of mouse SynCAM 2=== | ||
{{ABSTRACT_PUBMED_20739279}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/CADM2_MOUSE CADM2_MOUSE]] Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity). | |||
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==About this Structure== | ==About this Structure== | ||
[[3m45]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M45 OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020739279</ref><references group="xtra"/><references/> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Modis, Y.]] | [[Category: Modis, Y.]] | ||
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[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
Revision as of 23:25, 10 April 2013
Crystal structure of Ig1 domain of mouse SynCAM 2
Template:ABSTRACT PUBMED 20739279
Function
[CADM2_MOUSE] Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity).
About this Structure
3m45 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Fogel AI, Li Y, Giza J, Wang Q, Lam TT, Modis Y, Biederer T. N-glycosylation at the SynCAM immunoglobulin interface modulates synaptic adhesion. J Biol Chem. 2010 Aug 25. PMID:20739279 doi:10.1074/jbc.M110.120865