2oxe
From Proteopedia
(New page: 200px<br /> <applet load="2oxe" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oxe, resolution 2.80Å" /> '''Structure of the Hu...) |
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| - | [[Image:2oxe.gif|left|200px]]<br /> | + | [[Image:2oxe.gif|left|200px]]<br /><applet load="2oxe" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2oxe" size=" | + | |
caption="2oxe, resolution 2.80Å" /> | caption="2oxe, resolution 2.80Å" /> | ||
'''Structure of the Human Pancreatic Lipase-related Protein 2'''<br /> | '''Structure of the Human Pancreatic Lipase-related Protein 2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human pancreatic lipase-related protein 2 (HPLRP2) was found to be | + | Human pancreatic lipase-related protein 2 (HPLRP2) was found to be expressed in the pancreas, but its biochemical properties were not investigated in detail. A recombinant HPLRP2 was produced in insect cells and the yeast Pichia pastoris and purified by cation exchange chromatography. Its substrate specificity was investigated using pH-stat and monomolecular film techniques and various lipid substrates (triglycerides, diglycerides, phospholipids, and galactolipids). Lipase activity of HPLRP2 on trioctanoin was inhibited by bile salts and poorly restored by adding colipase. In vivo, HPLRP2 therefore seems unlikely to show any lipase activity on dietary fat. In human pancreatic lipase (HPL), residues R256, D257, Y267, and K268 are involved in the stabilization of the open conformation of the lid domain, which interacts with colipase. These residues are not conserved in HPLRP2. When the corresponding mutations (R256G, D257G, Y267F, and K268E) are introduced into HPL, the effects of colipase are drastically reduced in the presence of bile salts. This may explain why colipase has such weak effects on HPLRP2. HPLRP2 displayed a very low level of activity on phospholipid micelles and monomolecular films. Its activity on monogalactosyldiglyceride monomolecular film, which was much higher, was similar to the activity of guinea pig pancreatic lipase related-protein 2, which shows the highest galactolipase activity ever measured. The physiological role of HPLRP2 suggested by the present results is the digestion of galactolipids, the most abundant lipids occurring in plant cells, and therefore, in the vegetables that are part of the human diet. |
==About this Structure== | ==About this Structure== | ||
| - | 2OXE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2OXE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
[[Category: Bochkarev, A.]] | [[Category: Bochkarev, A.]] | ||
[[Category: Butler-Cole, C.]] | [[Category: Butler-Cole, C.]] | ||
[[Category: Davis, T.]] | [[Category: Davis, T.]] | ||
[[Category: Dhe-Paganon, S.]] | [[Category: Dhe-Paganon, S.]] | ||
| - | [[Category: Edwards, A | + | [[Category: Edwards, A M.]] |
| - | [[Category: Jr., P | + | [[Category: Jr., P J.Finerty.]] |
[[Category: Kozieradzki, I.]] | [[Category: Kozieradzki, I.]] | ||
| - | [[Category: SGC, Structural | + | [[Category: SGC, Structural Genomics Consortium.]] |
[[Category: Seitova, A.]] | [[Category: Seitova, A.]] | ||
[[Category: Sundstrom, M.]] | [[Category: Sundstrom, M.]] | ||
| - | [[Category: Walker, J | + | [[Category: Walker, J R.]] |
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:37 2008'' |
Revision as of 16:23, 21 February 2008
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Structure of the Human Pancreatic Lipase-related Protein 2
Overview
Human pancreatic lipase-related protein 2 (HPLRP2) was found to be expressed in the pancreas, but its biochemical properties were not investigated in detail. A recombinant HPLRP2 was produced in insect cells and the yeast Pichia pastoris and purified by cation exchange chromatography. Its substrate specificity was investigated using pH-stat and monomolecular film techniques and various lipid substrates (triglycerides, diglycerides, phospholipids, and galactolipids). Lipase activity of HPLRP2 on trioctanoin was inhibited by bile salts and poorly restored by adding colipase. In vivo, HPLRP2 therefore seems unlikely to show any lipase activity on dietary fat. In human pancreatic lipase (HPL), residues R256, D257, Y267, and K268 are involved in the stabilization of the open conformation of the lid domain, which interacts with colipase. These residues are not conserved in HPLRP2. When the corresponding mutations (R256G, D257G, Y267F, and K268E) are introduced into HPL, the effects of colipase are drastically reduced in the presence of bile salts. This may explain why colipase has such weak effects on HPLRP2. HPLRP2 displayed a very low level of activity on phospholipid micelles and monomolecular films. Its activity on monogalactosyldiglyceride monomolecular film, which was much higher, was similar to the activity of guinea pig pancreatic lipase related-protein 2, which shows the highest galactolipase activity ever measured. The physiological role of HPLRP2 suggested by the present results is the digestion of galactolipids, the most abundant lipids occurring in plant cells, and therefore, in the vegetables that are part of the human diet.
About this Structure
2OXE 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
Human pancreatic lipase-related protein 2 is a galactolipase., Sias B, Ferrato F, Grandval P, Lafont D, Boullanger P, De Caro A, Leboeuf B, Verger R, Carriere F, Biochemistry. 2004 Aug 10;43(31):10138-48. PMID:15287741
Page seeded by OCA on Thu Feb 21 18:23:37 2008
Categories: Homo sapiens | Single protein | Triacylglycerol lipase | Arrowsmith, C H. | Bochkarev, A. | Butler-Cole, C. | Davis, T. | Dhe-Paganon, S. | Edwards, A M. | Jr., P J.Finerty. | Kozieradzki, I. | SGC, Structural Genomics Consortium. | Seitova, A. | Sundstrom, M. | Walker, J R. | Weigelt, J. | CA | CL | Glycoprotein | Hydrolase | Lipid degradation | Pancreatic lipase | Sgc | Structural genomics consortium
