2ppl

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|PDB= 2ppl |SIZE=350|CAPTION= <scene name='initialview01'>2ppl</scene>, resolution 2.20&Aring;
|PDB= 2ppl |SIZE=350|CAPTION= <scene name='initialview01'>2ppl</scene>, resolution 2.20&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
|GENE= PNLIPRP1, PLRP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= PNLIPRP1, PLRP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=[[2oxe|2OXE]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ppl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ppl OCA], [http://www.ebi.ac.uk/pdbsum/2ppl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ppl RCSB]</span>
}}
}}
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[[Category: Walker, J R.]]
[[Category: Walker, J R.]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
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[[Category: CA]]
 
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[[Category: NA]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: lipid degradation]]
[[Category: lipid degradation]]
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[[Category: structural genomics consortium]]
[[Category: structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:15:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:06 2008''

Revision as of 01:39, 31 March 2008


PDB ID 2ppl

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: ,
Gene: PNLIPRP1, PLRP1 (Homo sapiens)
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Related: 2OXE


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Human Pancreatic lipase-related protein 1


Overview

We have isolated cDNAs coding for two novel human pancreatic lipase (hPL)-related human proteins, referred to as hPL-related proteins 1 and 2 (hPLRP1 and hPLRP2) and for hPL. The two novel proteins show an amino acid sequence identity to hPL of 68 and 65% for hPLRP1 and 2, respectively. All three proteins are secreted into the medium after transfection of COS cells with the corresponding cDNAs. The size of the three expressed proteins is similar and ranges between 45 and 50 kDa. The expressed hPLRP2 shows a lipolytic activity that is, however, in contrast to that of hPL only marginally dependent on the presence of colipase, whereas hPLRP1 shows no activity in this assay. A Northern analysis of normal human pancreas mRNA shows that the expression levels of hPLRP1 and hPLRP2 are about 4-fold and 24-fold lower, respectively, than that of hPL. hPLRP2 is, additionally, most closely related to a lipase reported to be expressed in mouse T-cells. A comparison of the sequences of the three proteins with sequences described as pancreatic lipases of other animal species shows three subfamilies of closer kinship. This suggests that the two novel proteins also exist in other species and that some of the sequences reported to be pancreatic lipase might more likely be the orthologues of hPLRP1 or hPLRP2 in those species.

About this Structure

2PPL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity., Giller T, Buchwald P, Blum-Kaelin D, Hunziker W, J Biol Chem. 1992 Aug 15;267(23):16509-16. PMID:1379598

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