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PDBsum entry 3abh

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protein Protein-protein interface(s) links
Endocytosis PDB id
3abh

 

 

 

 

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Contents
Protein chains
288 a.a. *
Waters ×551
* Residue conservation analysis
PDB id:
3abh
Name: Endocytosis
Title: Crystal structure of the efc/f-bar domain of human pacsin2/syndapin ii (2.0 a)
Structure: Protein kinasE C and casein kinase substrate in neurons protein 2. Chain: a, b. Fragment: efc/f-bar domain. Synonym: pacsin2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pacsin2. Expressed in: cell free system.
Resolution:
2.00Å     R-factor:   0.234     R-free:   0.271
Authors: A.Shimada,M.Shirouzu,K.Hanawa-Suetsugu,T.Terada,T.Umehara,S.Suetsugu, M.Yamamoto,S.Yokoyama
Key ref: A.Shimada et al. (2010). Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II. Febs Lett, 584, 1111-1118. PubMed id: 20188097
Date:
11-Dec-09     Release date:   14-Apr-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UNF0  (PACN2_HUMAN) -  Protein kinase C and casein kinase substrate in neurons protein 2 from Homo sapiens
Seq:
Struc:
486 a.a.
288 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Febs Lett 584:1111-1118 (2010)
PubMed id: 20188097  
 
 
Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.
A.Shimada, K.Takano, M.Shirouzu, K.Hanawa-Suetsugu, T.Terada, K.Toyooka, T.Umehara, M.Yamamoto, S.Yokoyama, S.Suetsugu.
 
  ABSTRACT  
 
The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21549705 D.Ruffell (2011).
Featuring… Shiro Suetsugu Winner of the 2011 FEBS Letters Young Group Leader Award.
  FEBS Lett, 585, 1504-1505.  
21059849 R.Zaidel-Bar, M.J.Joyce, A.M.Lynch, K.Witte, A.Audhya, and J.Hardin (2010).
The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesis.
  J Cell Biol, 191, 761-769.  
20435640 S.Suetsugu (2010).
The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins.
  J Biochem, 148, 1.  
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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