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PDBsum entry 2zmv

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protein Protein-protein interface(s) links
Transport protein PDB id
2zmv

 

 

 

 

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Contents
Protein chains
202 a.a. *
* Residue conservation analysis
PDB id:
2zmv
Name: Transport protein
Title: Crystal structure of synbindin
Structure: Trafficking protein particle complex subunit 4. Chain: a, b. Synonym: synbindin, trs23 homolog, hematopoietic stem/progenitor cell protein 172. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: trappc4, sbdn, cgi-104, hspc172, ptd009. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.80Å     R-factor:   0.245     R-free:   0.290
Authors: F.Fan
Key ref: S.Fan et al. (2009). Crystal structure of human synbindin reveals two conformations of longin domain. Biochem Biophys Res Commun, 378, 338-343. PubMed id: 18466758
Date:
21-Apr-08     Release date:   01-Jul-08    
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y296  (TPPC4_HUMAN) -  Trafficking protein particle complex subunit 4 from Homo sapiens
Seq:
Struc:
219 a.a.
202 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Biochem Biophys Res Commun 378:338-343 (2009)
PubMed id: 18466758  
 
 
Crystal structure of human synbindin reveals two conformations of longin domain.
S.Fan, Z.Wei, H.Xu, W.Gong.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19889231 M.Vedovato, V.Rossi, J.B.Dacks, and F.Filippini (2009).
Comparative analysis of plant genomes allows the definition of the "Phytolongins": a novel non-SNARE longin domain protein family.
  BMC Genomics, 10, 510.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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