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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Solution Structure of Synbindin Atypical PDZ Domain and Interaction with Syndecan-2

Author(s): Shilong Fan, Yingang Feng, Zhiyi Wei, Bin Xia and Weimin Gong

Volume 16, Issue 2, 2009

Page: [189 - 195] Pages: 7

DOI: 10.2174/092986609787316342

Price: $65


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 αA helix and the signature sequence Gly-Ψ-Gly-Ψ. 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.

Keywords: Synbindin, syndecan, PDZ domain, NMR, protein interaction

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