Structural highlights
Function
[TPPC4_HUMAN] May play a role in vesicular transport from endoplasmic reticulum to Golgi.
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 PubMed
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.
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
- ↑ Fan S, Wei Z, Xu H, Gong W. Crystal structure of human synbindin reveals two conformations of longin domain. Biochem Biophys Res Commun. 2009 Jan 16;378(3):338-43. Epub 2008 May 6. PMID:18466758 doi:http://dx.doi.org/10.1016/j.bbrc.2008.04.143