2zmv | pdb_00002zmv
From Proteopedia
Structural highlights
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 PubMedTransport 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. Crystal structure of human synbindin reveals two conformations of longin domain.,Fan S, Wei Z, Xu H, Gong W Biochem Biophys Res Commun. 2009 Jan 16;378(3):338-43. Epub 2008 May 6. PMID:18466758[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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