title: Crystal structure of human synbindin reveals two conformations of longin domain.
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.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Shilong
authors.initials: S
authors.lastname: Fan
authors.forename: Zhiyi
authors.initials: Z
authors.lastname: Wei
authors.forename: Hang
authors.initials: H
authors.lastname: Xu
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D054731:PDZ Domains; D011487:Protein Conformation; D033921:Vesicular Transport Proteins / Q000737:chemistry*
chemical_list: D009419:Nerve Tissue Proteins; C534479:TRAPPC4 protein, human; D033921:Vesicular Transport Proteins