3poy
From Proteopedia
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{{STRUCTURE_3poy| PDB=3poy | SCENE= }} | {{STRUCTURE_3poy| PDB=3poy | SCENE= }} | ||
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===Crystal Structure of the alpha-Neurexin-1 ectodomain, LNS 2-6=== | ===Crystal Structure of the alpha-Neurexin-1 ectodomain, LNS 2-6=== | ||
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{{ABSTRACT_PUBMED_21620717}} | {{ABSTRACT_PUBMED_21620717}} | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN]] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom. | ||
==About this Structure== | ==About this Structure== | ||
[[3poy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3POY OCA]. | [[3poy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3POY OCA]. | ||
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| - | ==See Also== | ||
| - | *[[Neurexin|Neurexin]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021620717</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021620717</ref><references group="xtra"/><references/> |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Comoletti, D.]] | [[Category: Comoletti, D.]] | ||
Revision as of 09:20, 19 June 2013
Contents |
Crystal Structure of the alpha-Neurexin-1 ectodomain, LNS 2-6
Template:ABSTRACT PUBMED 21620717
Function
[NRX1A_BOVIN] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.
About this Structure
3poy is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
- Miller MT, Mileni M, Comoletti D, Stevens RC, Harel M, Taylor P. The Crystal Structure of the alpha-Neurexin-1 Extracellular Region Reveals a Hinge Point for Mediating Synaptic Adhesion and Function. Structure. 2011 Jun 8;19(6):767-78. Epub 2011 May 27. PMID:21620717 doi:10.1016/j.str.2011.03.011
