3OK8

I-BAR OF PinkBAR

Summary for 3OK8

• Entry DOI: 10.2210/pdb3ok8/pdb
• Descriptor: Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2, GLYCEROL (3 entities in total)
• Functional Keywords: i-bar, protein binding
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 2
• Total formula weight: 52710.41

Authors

Boczkowska, M.,Rebowski, G.,Saarikangas, J.,Lappalainen, P.,Dominguez, R. (deposition date: 2010-08-24, release date: 2011-07-13, Last modification date: 2024-02-21)

Primary citation

Pykalainen, A.,Boczkowska, M.,Zhao, H.,Saarikangas, J.,Rebowski, G.,Jansen, M.,Hakanen, J.,Koskela, E.V.,Peranen, J.,Vihinen, H.,Jokitalo, E.,Salminen, M.,Ikonen, E.,Dominguez, R.,Lappalainen, P.
Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures.
Nat.Struct.Mol.Biol., 18:902-907, 2011

PubMed Abstract: Bin/amphipysin/Rvs (BAR)-domain proteins sculpt cellular membranes and have key roles in processes such as endocytosis, cell motility and morphogenesis. BAR domains are divided into three subfamilies: BAR- and F-BAR-domain proteins generate positive membrane curvature and stabilize cellular invaginations, whereas I-BAR-domain proteins induce negative curvature and stabilize protrusions. We show that a previously uncharacterized member of the I-BAR subfamily, Pinkbar, is specifically expressed in intestinal epithelial cells, where it localizes to Rab13-positive vesicles and to the plasma membrane at intercellular junctions. Notably, the BAR domain of Pinkbar does not induce membrane tubulation but promotes the formation of planar membrane sheets. Structural and mutagenesis analyses reveal that the BAR domain of Pinkbar has a relatively flat lipid-binding interface and that it assembles into sheet-like oligomers in crystals and in solution, which may explain its unique membrane-deforming activity.

PubMed: 21743456
DOI: 10.1038/nsmb.2079

Experimental method

X-RAY DIFFRACTION (2.25 Å)