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pubmed-article:18466758pubmed:abstractTextTransport 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.lld:pubmed
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pubmed-article:18466758pubmed:authorpubmed-author:GongWeiminWlld:pubmed
pubmed-article:18466758pubmed:authorpubmed-author:WeiZhiyiZlld:pubmed
pubmed-article:18466758pubmed:authorpubmed-author:XuHangHlld:pubmed
pubmed-article:18466758pubmed:authorpubmed-author:FanShilongSlld:pubmed
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pubmed-article:18466758pubmed:pagination338-43lld:pubmed
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pubmed-article:18466758pubmed:year2009lld:pubmed
pubmed-article:18466758pubmed:articleTitleCrystal structure of human synbindin reveals two conformations of longin domain.lld:pubmed
pubmed-article:18466758pubmed:affiliationSchool of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.lld:pubmed
pubmed-article:18466758pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18466758pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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