Structural highlights
Function
TPPC4_HUMAN May play a role in vesicular transport from endoplasmic reticulum to Golgi.
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
Synbindin is one component of Transport protein particle (TRAPP) complexes. In the hippocampal neurons, synbindin binds syndecan-2 by its atypical PDZ domain (APD) and may regulate the formation of dendritic spines. To investigate the interaction of synbindin and syndecan-2, we determined the solution structure of the synbindin APD by NMR. The structure of APD is different from the classical canonical PDZ domains by lacking the typical alphaA helix and the signature sequence Gly-Psi-Gly-Psi. These differences indicate that APD may not bind syndecan-2 with the typical binding mode of other PDZ domain proteins. In NMR titration experiments, APD do not bind with the C-terminal TKEFYA peptide of syndecan-2, but can interact with the 32-residue cytoplasmic domain of syndecan-2 very weakly.
Solution structure of synbindin atypical PDZ domain and interaction with syndecan-2.,Fan S, Feng Y, Wei Z, Xia B, Gong W Protein Pept Lett. 2009;16(2):189-95. PMID:19200043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fan S, Feng Y, Wei Z, Xia B, Gong W. Solution structure of synbindin atypical PDZ domain and interaction with syndecan-2. Protein Pept Lett. 2009;16(2):189-95. PMID:19200043
