Syntaxin-binding protein
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Function == | == Function == | ||
| - | '''Syntaxin-binding protein'''s (STXBP) are involved in the regulation of synaptic vesicle docking and fusion. '''STXBP1''' participates in synaptic vesicle fusion via dual roles: as a docking/chaperone protein by binding [[Syntaxin]]-1 and as a fusion protein that binds SNARE complexes in a [[Syntaxin]]-1 N-peptide-dependent manner<ref>PMID:21193638</ref>. '''STXBP2''' binds SNARE proteins. | + | '''Syntaxin-binding protein'''s (STXBP) are involved in the regulation of synaptic vesicle docking and fusion. '''STXBP1''' participates in synaptic vesicle fusion via dual roles: as a docking/chaperone protein by binding [[Syntaxin]]-1 and as a fusion protein that binds SNARE complexes in a [[Syntaxin]]-1 N-peptide-dependent manner<ref name="stxbp">PMID:21193638</ref>. '''STXBP2''' binds SNARE proteins. |
== Structural highlights == | == Structural highlights == | ||
| - | Syntaxin-binding protein 1 interaction with the N-terminal peptide of syntaxin-1 which forms part of the SNARE complex shows the peptide forming a tight loop with numerous intermolecular hydrogen bonds. The STXBP1 and the syntaxin peptide interact via numerous electrostatic and polar interactions<ref | + | Syntaxin-binding protein 1 interaction with the N-terminal peptide of syntaxin-1 which forms part of the SNARE complex shows the peptide forming a tight loop with numerous intermolecular hydrogen bonds. The STXBP1 and the syntaxin peptide interact via numerous electrostatic and polar interactions<ref name="stxbp"/>. |
</StructureSection> | </StructureSection> | ||
Revision as of 09:13, 6 December 2018
| |||||||||||
3D structures of syntaxin-binding protein
Updated on 06-December-2018
References
- ↑ 1.0 1.1 Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. Proc Natl Acad Sci U S A. 2010 Dec 30. PMID:21193638 doi:10.1073/pnas.0914906108
