3ipd
From Proteopedia
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{{STRUCTURE_3ipd| PDB=3ipd | SCENE= }} | {{STRUCTURE_3ipd| PDB=3ipd | SCENE= }} | ||
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===Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21=== | ===Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21=== | ||
+ | {{ABSTRACT_PUBMED_19571812}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/SNP25_RAT SNP25_RAT]] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [[http://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT]] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [[http://www.uniprot.org/uniprot/STX1A_RAT STX1A_RAT]] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. | |
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==About this Structure== | ==About this Structure== | ||
- | + | [[3ipd]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hd9 3hd9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IPD OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019571812</ref><references group="xtra"/><references/> |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Jahn, R.]] | [[Category: Jahn, R.]] | ||
Line 30: | Line 17: | ||
[[Category: Weber, G.]] | [[Category: Weber, G.]] | ||
[[Category: 4-helical bundle]] | [[Category: 4-helical bundle]] | ||
- | [[Category: Acetylation]] | ||
- | [[Category: Alternative splicing]] | ||
[[Category: Cell junction]] | [[Category: Cell junction]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
[[Category: Coiled coil]] | [[Category: Coiled coil]] | ||
- | [[Category: Cytoplasm]] | ||
[[Category: Cytoplasmic vesicle]] | [[Category: Cytoplasmic vesicle]] | ||
[[Category: Exocytosis]] | [[Category: Exocytosis]] | ||
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[[Category: Transport]] | [[Category: Transport]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 3 15:31:34 2009'' |
Revision as of 09:44, 27 March 2013
Contents |
Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21
Template:ABSTRACT PUBMED 19571812
Function
[SNP25_RAT] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [STX1A_RAT] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
About this Structure
3ipd is a 8 chain structure with sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 3hd9. Full crystallographic information is available from OCA.
Reference
- Stein A, Weber G, Wahl MC, Jahn R. Helical extension of the neuronal SNARE complex into the membrane. Nature. 2009 Jul 23;460(7254):525-8. Epub 2009 Jul 1. PMID:19571812 doi:10.1038/nature08156
Categories: Rattus norvegicus | Jahn, R. | Stein, A. | Wahl, M C. | Weber, G. | 4-helical bundle | Cell junction | Cell membrane | Coiled coil | Cytoplasmic vesicle | Exocytosis | Lipoprotein | Membrane | Membrane fusion | Membrane protein | Neurotransmitter transport | Palmitate | Phosphoprotein | Synapse | Synaptosome | Transmembrane | Transport | Transport protein