2oxe
From Proteopedia
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'''Structure of the Human Pancreatic Lipase-related Protein 2''' | '''Structure of the Human Pancreatic Lipase-related Protein 2''' | ||
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[[Category: Walker, J R.]] | [[Category: Walker, J R.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Lipid degradation]] |
| - | [[Category: | + | [[Category: Pancreatic lipase]] |
| - | [[Category: | + | [[Category: Sgc]] |
| - | [[Category: | + | [[Category: Structural genomics consortium]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:52:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:52, 4 May 2008
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. 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 Sun May 4 11:52:08 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. | Glycoprotein | Hydrolase | Lipid degradation | Pancreatic lipase | Sgc | Structural genomics consortium
