2ppl

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spinqualitylabelsall models 2ppl, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 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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