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| - | [[Image:1bu8.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bu8| PDB=1bu8 | SCENE= }} | | {{STRUCTURE_1bu8| PDB=1bu8 | SCENE= }} |
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| - | '''RAT PANCREATIC LIPASE RELATED PROTEIN 2'''
| + | ===RAT PANCREATIC LIPASE RELATED PROTEIN 2=== |
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| - | ==Overview==
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| - | The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2). Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties. PLRP1 has no known activity. PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation. To begin understanding the structural explanations for these functional differences, we solved the crystal structure of rat (r)PLRP2 and further characterized its kinetic properties. The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain. The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation. When we reexamined this issue with tripropionin as substrate, rPLRP2 exhibited interfacial activation. Because the active site topology of rPLRP2 resembled that of human PTL, we predicted and demonstrated that the lipase inhibitors E600 and tetrahydrolipstatin inhibit rPLRP2. Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique. With this assay, we showed for the first time that rPLRP2 prefers phosphatidylglycerol and ethanolamine over phosphatidylcholine. In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9822688}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9822688 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9822688}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipid degradation]] | | [[Category: Lipid degradation]] |
| | [[Category: Pancreatic lipase]] | | [[Category: Pancreatic lipase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:57:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:43:47 2008'' |
Revision as of 16:43, 30 June 2008
Template:STRUCTURE 1bu8
RAT PANCREATIC LIPASE RELATED PROTEIN 2
Template:ABSTRACT PUBMED 9822688
About this Structure
1BU8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure and activity of rat pancreatic lipase-related protein 2., Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M, J Biol Chem. 1998 Nov 27;273(48):32121-8. PMID:9822688
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