|PROSITE documentation PDOC50095|
The PLAT domain (after polycystin-1, lipoxygenase and α toxin) is an intracellular domain of ~150 residues. The PLAT domain can be found associated with other domains such as LRR, PKD (see <PDOC50093>), C-type lectin (see <PDOC00537>), GPS (see <PDOC50221>), lipase, lipoxygenase (see <PDOC00077>) prokaryotic zinc-dependent phospholipase C (see <PDOC00357>), LCCL (see <PDOC50820>) or SRCR (see <PDOC00348>), It has been proposed that the PLAT domain may be involved in protein-protein and protein-lipid interaction [1,2].
The three-dimensional structure of the PLAT domain is known for several proteins. The domain is a β-sandwich composed of two sheets of four strands each (see <PDB:1LOX>). The most highly conserved regions of the PLAT domain coincide with the β-strands. Most of the highly conserved residues are buried residues. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth β-strand of all eukaryotic PLAT domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site within the PLAT domain .
Some proteins known to contain a PLAT domain are listed below:
The profile we developed covers the entire PLAT domain.Last update:
April 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Bateman A., Sandford R.|
|Title||The PLAT domain: a new piece in the PKD1 puzzle.|
|Source||Curr. Biol. 9:R588-R590(1999).|
|2||Authors||Delrieu I., Waller C.C., Mota M.M., Grainger M., Langhorne J., Holder A.A.|
|Title||PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes.|
|Source||Mol. Biochem. Parasitol. 121:11-20(2002).|