Biology:PLAT domain
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PLAT/LH2 domain | |||||||||
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Structure of the lipase-procolipase complex.[1] | |||||||||
Identifiers | |||||||||
Symbol | PLAT | ||||||||
Pfam | PF01477 | ||||||||
InterPro | IPR001024 | ||||||||
SMART | SM00308 | ||||||||
PROSITE | PDOC50095 | ||||||||
SCOP2 | 1lpa / SCOPe / SUPFAM | ||||||||
OPM superfamily | 221 | ||||||||
OPM protein | 3swz | ||||||||
CDD | cd00113 | ||||||||
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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.
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
- ↑ "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography". Nature 362 (6423): 814–20. April 1993. doi:10.1038/362814a0. PMID 8479519.
- ↑ 2.0 2.1 "The PLAT domain: a new piece in the PKD1 puzzle". Curr. Biol. 9 (16): R588–90. 1999. doi:10.1016/S0960-9822(99)80380-7. PMID 10469604.
- ↑ "A latrophilin/CL-1-like GPS domain in polycystin-1". Curr. Biol. 9 (16): R585–8. August 1999. doi:10.1016/S0960-9822(99)80379-0. PMID 10469603.
- ↑ "PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes". Mol. Biochem. Parasitol. 121 (1): 11–20. 2002. doi:10.1016/S0166-6851(02)00016-6. PMID 11985859.
- ↑ "Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1". Biochemistry 40 (25): 7509–7517. 2001. doi:10.1021/bi002893d. PMID 11412104.
Original source: https://en.wikipedia.org/wiki/PLAT domain.
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