Reference: Fan S, et al. (2009) Crystal structure of human synbindin reveals two conformations of longin domain. Biochem Biophys Res Commun 378(3):338-43

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Abstract


Transport protein particle (TRAPP) is a large multiprotein complex that involves in ER-to-Golgi and intra-Golgi traffic. Synbindin, the human ortholog of yeast Trs23, is one component of the TRAPP complexes. In the hippocampal neurons the synbindin/syndecan complex is involved in synaptic membrane trafficking and thereby regulates the formation of dendritic spines. Here we present the three-dimensional structure of human synbindin, which contains a longin domain (LD) and an atypical PDZ domain (APD). In the crystal, synbindin forms a hexamer, in which the LD forms two different conformations and the APD is quite disordered. These conformational changes of synbindin suggest a possible interaction mode of the LD.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Fan S, Wei Z, Xu H, Gong W
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