Structural highlights
Function
[APBA1_HUMAN] Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Members of the X11/Mint family of multidomain adaptor proteins are composed of a divergent N terminus, a conserved PTB domain and a pair of C-terminal PDZ domains. Many proteins can interact with the PDZ tandem of X11 proteins, although the mechanism of such interactions is unclear. Here we show that the highly conserved C-terminal tail of X11alpha folds back and inserts into the target-binding groove of the first PDZ domain. The binding of this tail occludes the binding of other target peptides. This autoinhibited conformation of X11 requires that the two PDZ domains and the entire C-terminal tail be covalently connected to form an integral structural unit. The autoinhibited conformation of the X11 PDZ tandem provides a mechanistic explanation for the unique target-binding properties of the protein and hints at potential regulatory mechanisms for the X11-target interactions.
Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem.,Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M Nat Struct Mol Biol. 2005 Aug;12(8):722-8. Epub 2005 Jul 10. PMID:16007100[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M. Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat Struct Mol Biol. 2005 Aug;12(8):722-8. Epub 2005 Jul 10. PMID:16007100 doi:http://dx.doi.org/10.1038/nsmb958
