PLAT domain

In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain[2] or LH2 (Lipoxygenase homology) domain.[3] The known structure of pancreatic lipase shows this domain binds to procolipase Pfam PF01114, which mediates membrane association.

PLAT/LH2 domain
Structure of the lipase-procolipase complex.[1]
Identifiers
SymbolPLAT
PfamPF01477
InterProIPR001024
SMARTSM00308
PROSITEPDOC50095
SCOP21lpa / SCOPe / SUPFAM
OPM superfamily221
OPM protein3swz
CDDcd00113
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

This domain forms a beta-sandwich composed of two β-sheets of four β-strands each.[2][4][5]

Human proteins containing this domain

ALOX12; ALOX12B; ALOX12P2; ALOX15; ALOX15B; ALOX5; ALOXE3; LIPC; LIPG; LOXHD1; LPL; PKD1; PKD1L1; PKD1L2; PKD1L3; PKDREJ; PNLIP; PNLIPRP1; PNLIPRP2; PNLIPRP3; RAB6IP1;

References

  1. van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C (April 1993). "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography". Nature. 362 (6423): 814–20. doi:10.1038/362814a0. PMID 8479519. S2CID 4305832.
  2. Bateman A, Sandford R (1999). "The PLAT domain: a new piece in the PKD1 puzzle". Curr. Biol. 9 (16): R588–90. doi:10.1016/S0960-9822(99)80380-7. PMID 10469604. S2CID 15018010.
  3. Ponting CP, Hofmann K, Bork P (August 1999). "A latrophilin/CL-1-like GPS domain in polycystin-1". Curr. Biol. 9 (16): R585–8. doi:10.1016/S0960-9822(99)80379-0. PMID 10469603. S2CID 17252179.
  4. Delrieu I, Waller CC, Mota MM, Grainger M, Langhorne J, Holder AA (2002). "PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes". Mol. Biochem. Parasitol. 121 (1): 11–20. doi:10.1016/S0166-6851(02)00016-6. PMID 11985859.
  5. Minor W, Tomchick DR, Phan P, Cymborowski M, Holman TR (2001). "Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1". Biochemistry. 40 (25): 7509–7517. doi:10.1021/bi002893d. PMID 11412104.
This article incorporates text from the public domain Pfam and InterPro: IPR001024
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